Product Search for novus: Novus Biologicals

NB100-122

HIF-2 alpha/EPAS1 Antibody - BSA Free

(37 Reviews)

(781 Publications)

0.1 ml

NB100-122

WNT11 is induced by hypoxia or hypoxic mimetics in different cell types. Immunoblot analyses of HeLa cells under normal air or hypoxia for 24 hrs. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep21520) licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>HIF-1alpha is the predominant transcriptional regulator of WNT11 expression during hypoxia. EMSCs isolated from the indicated mouse genotypes were infected with lentivirus expressing GFP or Cre recombinase. Non-infected cells and GFP infected cells served as controls. Immunoblot analyses of EMSCs derived from the indicated genotypes treated with 0.1 mM DMOG for 24 hrs. Attenuated WNT11 expression in Hif-1alpha KO EMSCs (lenti-Cre infected Hif-1af/f). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep21520) licensed under a CC-BY license.

<b>Orthogonal Strategies Validation. </b>Formalin-fixed paraffin-embedded tissue sections of human placenta were probed for HIF-2 alpha/EPAS1 mRNA (ACD RNAScope Probe, catalog #410598; Fast Red chromogen, ACD catalog # 322750). Adjacent tissue section was processed for immunohistochemistry using Rabbit Polyclonal (Novus Biologicals catalog # NB100-122) at 1:100 dilution with one-hour incubation at room temperature followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody (Catalog # VC003) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to trophoblastic cells.

Expression of hypoxia-inducible alpha subunits in normal and diseased lung tissue. HIF-2alpha expression are more evident in fibroblasts from idiopathic pulmonary fibrosis (d) than from lung tissue affected by other inflammatory conditions (i.e. chronic bronchitis, panel e) or normal lung tissue (f); as demonstrated by a higher proportion of positive fibroblasts (open arrows) than negative ones (solid black arrows). Image collected and cropped by CiteAb from the following publication (//respiratory-research.biomedcentral.com/articles/10.1186/s12931-019-1100-4) licensed under a CC-BY license.

Image shows a specific band for HIF-2 alpha in 0.5 mg/mL of hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

<b>Genetic Strategies Validation. </b>Immunoblot validation of HIF2A and PHD2 KO clones using HIF2A (#NB100-122; dilution: 1/300), PHD2 (#NB100-137; dilution: 1/500). To blot HIFs factor cells were first pre-treated for 5 h with CoCl2 300 uM before protein extraction, a condition that promotes HIF factor accumulation. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-06988-3) licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>HIF-2 alpha in human retinal and choroidal primary endothelia lysates using .. Image from verified customer review.

<b>Biological Strategies Validation. </b>HIF-2 alpha in MDA-MB-231 cell lysate (overexpression and endogenous samples) using . did not react to HIF-1 alpha overexpression. Image from verified customer review.

Induced WNT11 expression with tumor hypoxia and WNT11 regulates tumor growth. Bevacizumab increased expression of HIF-1alpha and HIF-2alpha and WNT11. First 10 lanes are control tumors, and the last 10 lanes are tumors from bevacizumab-treated animals. Lysates from whole tissue and nuclei are indicated. Alpha -Tubulin, actin and lamin A/C are loading controls. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep21520) licensed under a CC-BY license.

MDA-MB-231 cells were exposed to 20% or 1% O2 for 16 hours, and chromatin immunoprecipitation (ChIP) was performed with the indicated antibody (Ab). Primers flanking the HIF binding site were used for qPCR. ChIP image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Lane 1: Cobalt chloride treated COS7 nuclear extracts. Lane 2: Untreated COS7 nuclear extracts.

786-O cells without or with VHL overexpression. Image from verified customer review.

<b>Biological Strategies Validation. </b>Analysis using the HRP conjugate of NB100-122. Detection of normoxic and hypoxic nuclear rat cell lysates.

HIF-2 alpha immunoreactivity in human cardiac myocytes stained with NB100-122.

Expression and correlation of 3 antibodies: HIF-1 alpha, HIF-2 alpha and HAF in ccRCC. (A, C & E) Positive nuclear staining to the 3 antibodies: HIF-1 alpha, HIF-2 alpha and HAF, in primary ccRCCs at high magnification (100X). (B, D & F) Heterogenous nuclear staining of 3 antibodies in a tumor at low magnification (20X). (G, H and I). Correlation of 3 antibodies with the Fuhrman grade.Citation: Ambrosetti D, Dufies M, Dadone B, Durand M, Borchiellini D, Amiel J, et al. (2018) The two glycolytic markers GLUT1 and MCT1 correlate with tumor grade and survival in clear-cell renal cell carcinoma. PLoS ONE 13(2): e0193477. //doi.org/10.1371/journal.pone.0193477

<b>Genetic Strategies Validation. </b>Reduction of HIF-2alpha levels leads to protection in UV-triggered apoptosis, but not for apoptosis caused by glucose and serum starvation in 786-O cells. Parental 786-O or those either stably expressing wild-type VHLp19 or stably infected with a control vector (pSuperRetro) or a pool of two HIF-2alpha shRNAs vectors [21] were grown to confluence and lysed. Cell alpha-tubulin.

Sp1 and HIFs contribute to the synergistic activation of multiple genes in OVSAYO cells under SSH.b) Activation of multiple genes under hypoxia is dependent on HIFs. Western blotting is also shown for HIFs. Data shown are the mean (n = 3) ± SD.

Manipulation of DNA methylation at HRE sequences alters HIF binding. (A) The Hypoxia Response Element (HRE) contains a CpG site that can be methylated which prevents HIF1 and HIF2 binding in vitro. EMSA of in vitro-translated HIF1 and HIF2 binding to 32P-labelled unmethylated and methylated HRE probes. Competition with 250X molar excess of unlabelled/unmethylated HRE probe (lanes 3, 7,12, 16) or unlabelled control HRE-free probe (lanes 4, 8, 13, 17). HIF1 and HIF2 complexes bound to unmethylated HRE or methylated HRE supershifted with anti-HIF1alpha (lanes 9 and 18) and anti-HIF2alpha (lanes 5 and 14). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-21524-5), licensed under a CC-BY licence.

Hypoxia and HIF-1 accumulation after DSS-treatment.Real time PCR of HIF-1alpha exon 2 (A) in RNA samples of hypoxic treated BMDM of wild type (HIF-1alpha+f/+f) and knockout (Lyz2-Cre/HIF-1alpha+f/+f) mice with 14 samples/group. Each bar represents the mean value +/- SEM. ***P 0.01 vs. normal thyroid; #P > 0.01 vs. normal thyroid; (d) Relative expression levels of HMGB1 in thyroid cancer. Total mRNA was extracted from thyroid cancer patients’ tissues and HMGB1 level determined by relative optical intensity (in arbitrary units, AU) of bands on RT-PCR. Each dot represented relative level of HMGB1 in an individual sample. *P > 0.01 vs. FTC; (e) HMGB1 expression level for differentiating thyroid cancer tissues from non-thyroid cancer tissues in our validated cohort; AUC: 96.7%, sensitivity: 88.9% and specificity: 96.2% in the validated cohort Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci and RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive and negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemical detection of HIF-1 alpha protein in human tissues. The nature of the tissue is indicated on top of each figure. Original magnifications are as follows: A, ×400; B, ×400; C, ×100; D, ×100; E, ×100; F, ×100; G, ×40; H, ×40. Image collected and cropped by CiteAb from the following open publication (//bmcgenet.biomedcentral.com/articles/10.1186/1471-2156-5-27), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ROS overproduction mediated apoptosis induced by combined treatment of DDP and HIF-1 alpha in PC-3 xenografts and cell culture. (a) ROS monitored by DHE (red) and nuclei by DAPI (blue) staining in PCa xenografts (scale bars, 50 µm). (b) MDA formation of PCa xenografts was examined after various treatments (c,d). PC-3 cells were treated with DDP, si-HIF-1 alpha plasmid, or both, in the presence or absence of NAC (5 mM) or DHLA (0.25 mM) for 24 h. Total lysates (c) and culture media (d) were used to detect cellular H2O2 level. (e,f) Western analysis for HIF-1 alpha as well as cleaved caspase-3 and PARP in PC-3 cells following various treatments. Data were presented as mean ± SD of three independent experiments. *p 2000 neurons/condition; one-way ANOVA with Bonferroni's multiple comparisons test). (B) PGD2 did not induce pRII in non-neuronal cells of the same cultures shown in A. (C) Time course of RII phosphorylation indicating long-lasting effects of PGD2 (10 µM) on sensory neurons. (D) Stimulation with PGD2 also results in phosphorylation of the ERK1/2 measured in the same cultures shown in D. (E) Representative experiment demonstrating that induction of RII phosphorylation is enhanced in TRPV1(+) neurons (total of 3664 neurons). Plots of respective controls are shown in S2 Fig. (F) Fold changes of pRII intensities in TRPV1(−) (grey bars) and TRPV1(+) (black bars) neurons after 1 min stimulation with 10 µM PGD2 (n = 3,>2000 neurons/condition, one-way ANOVA with Bonferroni's multiple comparisons test). (G) Co-labeling of TRPV1 and PTGDS revealing that PTGDS is expressed in neurons lacking TRPV1 (total of 9951 neurons, also refer to S2 Fig. for control plots). (H) Co-labeling of NF200 and PTGDS showing that PTGDS(+) neurons express NF200 (total of 12966 neurons, also refer to S2 Fig. for control plots).(I) Size distribution of PTGDS(+) (green), NF200(+) (red), and all sensory neurons (black) indicating that PTGDS(+) neurons are larger than other neurons. (J) Suggested pathway of interneuronal communication between subgroups of sensory neurons. Large-diameter mechanosensitive neurons express PTGDS resulting in the production of PGD2, which activates DP1 receptors present on nociceptive neurons expressing TRPV1. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0115731), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

SPOC1 is recruited to I-SceI-induced DSBs where it colocalizes with 53BP1. (A) In situ immunofluorescence studies with U2OS19 ptight13 GFP-LacR cells with a stably integrated I-SceI cleavage site flanked by lac operator repeats reveals localization of the GFP-lac repressor protein (GFP-LacR) at the lac-operator DNA sequences in the nucleus before (−I-SceI) and 16 h after I-SceI-induced (+ I-SceI) DSB. In contrast, SPOC1 (white) and 53BP1 (red) are distributed throughout the nucleus in the absence of I-Scel, and partially colocalized in naturally occurring repair foci. After I-SceI cleavage to generate DSBs, SPOC1 and 53BP1 colocalize at distinct foci, including the cleaved DNA adjacent to DNA-bound GFP-LacR. Proteins were visualized by immunostaining and confocal microscopy. Scale bars = 10 μm. (B) Quantitative analysis of SPOC1 recruitment to the 53BP1 and GFP-LacR positive lacO array before and 16 h after I-SceI induction. (C) Monitoring of the kinetics of SPOC1 and 53BP1 recruitment to DSBs between 0 and 24 h post-I-SceI induction. (D) Quantifying ATM kinase inhibitor-mediated effects on recruitment of SPOC1 and 53BP1 to DSBs as evident 16 h after I-SceI-induced cleavage. (E) SPOC1 and 53BP1 colocalize at a large discrete endogenous repair focus as observed in some non-irradiated U2OS cells by immunostaining. Scale bar = 10µm. Image collected and cropped by CiteAb from the following open publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gks868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Hypoxia reduces inflammatory signaling pathways and NLRP3 expression and induces autophagy in IECs. a HT-29 cells were subjected to normoxia and hypoxia at the indicated times in the absence or presence of 10 µg/ml LPS. Autophagy was measured by variations in the ratio of LC3-II/LC3-I and the total amount of LC3 (LC3-I plus LC3-II) relative to beta -actin. Results are representative of two independent experiments. b, c and d HT-29 cells were subjected to normoxia and hypoxia for the indicated periods in the absence or presence of 10 µg/ml LPS, followed by transcript analysis. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Results represent mean + s.e.m. of two independent experiments done in triplicate, *P < 0.05; **P < 0.01; ***P < 0.001; ns not significant. e HT-29 cells were subjected to normoxia or hypoxia in the presence and absence of 10 µg/ml LPS and 20 µM of MG132. Results are representative of two independent experiments. f and g Putative binding sites for HIF-1 alpha and NF-kappa B were found in the p62 f and NLRP3 g promoters using Genomatix software tools. Numbers under the boxes indicate the distance from the transcription start site. HT-29 cells were subjected to normoxia (21% O2) or hypoxia (0.2% O2) for 6 h and 24 h. ChIP analysis was performed using antibodies against HIF-1 alpha and NF-kappa B for immunoprecipitation. PCR was performed using the promoter-specific primers for the p62 f and NLRP3 g promoter binding sites of HIF-1 alpha and NF-kappa B. Aliquots taken prior to immunoprecipitation were used as input control. PCR products were run on 2% agarose gel. The results are representative of three independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28740109), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The FANCD2 NLS is required for the nuclear localization of a subset of FANCI.(A) FA-D2 patient cells or FA-D2 cells stably expressing FANCD2-WT were incubated in the absence (NT) or presence of MMC for 24 h, fixed, stained with rabbit polyclonal anti-FANCD2 or anti-FANCI antibody and counterstained with phalloidin and DAPI. AF-488, Alexa Fluor 488. (B) FA-D2 cells stably expressing LacZ, FANCD2-WT, FANCD2-∆N57, FANCD2-∆N100, and FANCD2-3N were incubated in the absence (NT) or presence of MMC for 24 h, fixed, and stained with rabbit polyclonal anti-FANCI antibody, and counterstained with phalloidin and DAPI. At least 300 cells were scored for cytoplasmic (Cyto.), nuclear (Nucl.), and both cytoplasmic and nuclear (Both) localization of FANCI. (C) COS-7 cells were transiently transfected with no DNA, FANCI-GFP, FANCI-GFP plus FANCD2-V5-WT, or FANCI-GFP plus FANCD2-V5-∆N57. Whole-cell lysates were immunoprecipitated with anti-V5 or anti-GFP antibodies and immune complexes immunoblotted with anti-GFP and anti-V5 antibodies. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24278431), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Analysis of microvascular density and HIF-1 alpha activity. Microvascular density of pulmonary tumors was significantly higher in hyperplastic (B) and tumoral lesions (D) of NNK/NTHi treated mice compared to the NNK treated mice (A, and C) detected by CD105 immunostaining (10X, scale bar = 100 μm). HIF-1 alpha immunostaining after NNK/NTHi combined treatment showed hot-spots of high stromal expression in tumors (F), and high expression in perivascular-peribronchiolar lymphocytes (H). In contrast, low, homogenous expression of HIF-1 alpha was detected in the tumors (E) and perivascular-peribronchiolar lymphocytes (G) of NNK treated mice (40X, scale bar = 25 μm). Image collected and cropped by CiteAb from the following open publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

JMJD2B expression increases in hepatic steatotic cell and animal models. (A) HepG2 cells were incubated with a mixture of palmitic acid (PA) and oleic acid (OA) (1:2 ratio) at 800 μM concentrations for 24 h, and intracellular triglyceride (TG) levels were analyzed by a TG assay kit. JMJD2B mRNA and protein levels were examined by qPCR and western blotting, respectively. Data represent means ± SEM of three independent experiments performed in triplicate. *p < 0.05 vs. no treatment. The full-length western blots corresponding to truncated blots are presented in Supplementary Figure S1A. (B) HepG2 cells were treated with T0901317 (10 μM) for 24 h, and intracellular triglyceride (TG) levels were measured by a TG assay kit. JMJD2B mRNA and protein levels were examined by qPCR and western blotting, respectively. Data represent means ± SEM of three independent experiments performed in triplicate. *p < 0.05 vs. no treatment. The full-length western blots are presented in Supplementary Figure S1B. (C) Total RNAs were isolated from the livers of HFD-induced obese mice. The JMJD2B mRNA levels were assessed by qPCR. Data represent means ± SEM of 5 mice. *p < 0.05 vs. ND mice. ND: normal diet. HFD: high fat diet. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30214048), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Protein expressions of intrarenal RAS components in two groups of mice. (A) Immunohistochemical analysis of intrarenal RAS expression position in the two groups of mice. AGT immunoreactivity in the proximal tubular cells, Ang II immunoreactivity in both glomerular and tubular cells, renin immunoreactivity in juxtaglomerular apparatus cells, ACE immunoreactivity in brush border membranes of proximal tubules as well as AT1 and AT2 immunoreactivity in the proximal tubules were increased in the HF group when compared to the control group. (B) Western blot analysis for protein expressions of intrarenal RAS components in the two groups of mice. (C) The histogram represents mean ± SD of the densitometric scans for the protein bands of angiotensinogen (AGT), angiotensin II (Ang II), renin, angiotensin converting enzyme (ACE), angiotensin II type 1 receptor (AT1), angiotensin II type 2 receptor (AT2) from five experiments, normalized by beta -actin. * P < 0.05 vs. control. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23570453), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$TAZ induces Tfam protein expression at the translational level.a The expression of mitochondrial biogenic factors, including Tfam, Ppargc1a (Pgc1 alpha ), Nrf1, and Nrf2, was analysed using quantitative reverse transcription (qRT)-PCR in the gastrocnemius muscle of wild-type (WT) and muscle-specific TAZ knockout (mKO) mice; n = 6 for each condition (Tfam; *p = 0.0498, Nrf1; *p = 0.0467). b Protein was analysed via immunoblotting to detect TAZ and the indicated mitochondrial biogenic factors in (a). Alpha-tubulin was used as the loading control. c RNA was isolated from the control (Con) and TAZ knockdown (KD) C2C12 myotubes, and the expression of the indicated mitochondrial biogenic factors was analysed using qRT-PCR. The experiments were performed in triplicate (Tfam; *p = 0.04). d Protein from the Con and TAZ KD C2C12 myotubes was assessed via immunoblotting to detect TAZ and mitochondrial biogenic factors. Beta-actin was used as the loading control. e RNA was isolated from WT, TAZ-knockout (KO), and TAZ-rescued (T) mouse embryonic fibroblasts (MEF), and the indicated mitochondrial biogenic factors were analysed via qRT-PCR. f Protein from WT, KO, and T MEF was assessed via immunoblotting to detect TAZ and the indicated mitochondrial biogenic factors. Beta-actin was used as the loading control. g Protein was isolated from the gastrocnemius muscle of WT and mKO mice and analysed via immunoblotting to detect TAZ, YAP, and proteins involved in the translation of both phosphorylated and total forms. Alpha-tubulin was used as the loading control. h Protein obtained from the Con and TAZ KD C2C12 myotubes was assessed via immunoblotting to observe TAZ and proteins involved in translation. Beta-actin was used as the loading control. i Protein was isolated from WT, KO, and T MEF and analysed via immunoblotting to detect TAZ and proteins involved in translation. Vinculin was used as the loading control. j The polysome profile of cells described in panel i was evaluated continuously by measuring absorbance at 254 nm. The 40S, 60S, 80S, and polysome fractions are denoted by the corresponding peaks. k The distribution of Tfam, Atp5d, and Gapdh mRNA from cells described in (j) across a density gradient was analysed using reverse transcription (RT)-PCR. bp = base pairs. For a, b, g 8 to 10-week-old mice were used. Data are presented as mean ± SEM for (a), mean ± SD for (c, e). Statistical significance was analysed via two-sided t-test for (a) and one-sided t-test for (c). One-way ANOVA with Tukey’s multiple comparison test was used for (e). Representative data was shown and experiments were performed at least twice with similar results for (b, d, f–i, k). Source data are provided as a Source data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35115527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Binding of TRF2 to viral DNA during HHV-6A/B infection.A) Schematic representation of the HHV-6A/B genome. The DR6 probe used for hybridization is shown in red. Uninfected and HHV-6A-infected HSB-2 cells (B-D) or uninfected and HHV-6B-infectd Molt-3 cells (E-F) were analyzed for TRF2 binding to viral DNA using ChIP. The input was hybridized with Alu probe to assess quantity of starting material. Anti-IgG (negative control), anti-PolII (positive control) or TRF2 antibodies were used for immunoprecipitation. B) QPCR detection of GAPDH DNA following ChIP. Results are expressed as fold increase over control IgG. C and E) Eluted DNA was hybridized with 32P-labeled Alu, telomeric (TTAGGG)3 or HHV-6A (DR6) probes. After hybridization the membranes were washed and exposed to X-ray films. D and F) Densitometric analysis of relative binding of TRF2 to telomeric and viral DNA. Results of one experiment representative of three are presented and are expressed as signal after normalization to input. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

miR-375 control on CIP2A-MYC pathway also contributes to p21 elevation. (A) p21, p53, RB, CIP2A, and MYC protein levels in MCF7 cells transfected with miR-375 inhibitor, -mimic, or NS control were measured by Western blot analysis. Tubulin expression was used as internal control. 25%, 50%, 100% amounts of untreated cell lysates were included to calibrate the semiquantitative measurement. (B) Transfection with miR-375-mimic significantly upregulated p21 mRNA in MCF7. Relative endogenous p21 mRNA levels were measured in MCF7 cells transfected with miR-375 inhibitor, -mimic, or NS control for 48 h using qRT-PCR. (C) CIP2A and MYC protein levels were effectively silenced by si-CIP2A transfection with 1 and 10 nM concentrations for 48 h. Increased p21 protein levels were detected in si-CIP2A dose-dependent manner. 10 nM of si-GFP was used as a control. (D) Protein levels of CIP2A, p53, and p21 in MCF7 cells transfected with si-p53 and/or miR-375-mimic were measured by Western blot analysis. (E) mRNA levels of p21 in MCF7 cells transfected with si-p53 and/or miR-375-mimic were measured by qRT-PCR. (F) Flow cytometry analysis demonstrates G1 arrest of MCF7 cells 48 h after transfection with miR-375-mimic compared to miR-375 inhibitor or NS control. The concentrations of siRNA or miRNA used in panels D, E, and F were 10 nM and 25 nM, respectively. (G) Schematic depiction of miR-375-mediated repression of CIP2A, E6, E6AP, and E7 in HPV16-positive cells that simultaneously increases tumor suppressor p53, p21, and RB, and causes cell cycle arrest. Results are expressed as mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, and ***p < 0.001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24708873), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effect of the four most common herbal formulas and single herbs on the phosphorylation of myosin light chain (MLC) protein.Briefly, A10 cells were treated with herbal formulas (A) or single herbs (B). Y27632 (Y10; 10 μM) and calyculin A (A50; 50 μg/ml) were used as negative and positive controls. Western blot analysis and staining with anti-phospho-MLC, anti-total-MLC, and anti-beta actin antibodies was then performed. Phospho-MLC, total-MLC, and beta actin were all obtained with their appropriate protein size bands. The relative Phospho-MLC intensity (%) was expressed as [(Phospho-MLC/total-MLC)drug treated/ (Phospho-MLC/total-MLC)cell only x 100%]. The Mean±SEM values for at least three independent experiments along with the representative western blot were performed. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0145109), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Silencing CIP2A caused decreased Cdk1 and Cdk2 proteins in 16E6‐expressing cells. A, Western blot analysis of CIP2A, Cdk4, Cdk6, cyclin D1, Cdk1, Cdk2, cyclin B1, cyclin A2 and cyclin E1 protein levels in cells expressing HPV‐16E6 transfected with CIP2A siRNA and then treated with PBS or 10 μg/mL bleomycin for 24 h. A representative of 3 independent experiments is shown. B, Quantification of all cell cycle‐related proteins. Data from 3 experiments are summarized. C, Relative mRNA levels of all cell cycle‐related genes determined by qRT‐PCR. Data from 3 experiments are summarized. *, P < .05; **, P < .01 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29893470), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effect of alcohol on TERT expression in liver tissues and KCs during ALD development.(a) TERT expression in liver tissues was performed by IHC analysis. Representative views from each group were presented (original magnification, ×40). (b) Total TERT mRNA and protein levels in liver tissue were analyzed by real-time PCR and western blot. The results are shown as relative expression against control expression without treatment. (c) Representative colocalization of TERT with macrophage CD68 immunoreactivity in liver tissue by using the double immunofluorescent (IF) analysis. (d) Total TERT mRNA and protein levels in KCs isolated from the liver were analyzed by real-time PCR and western blot. The results are shown as relative expression against control expression without treatment. (e) Quantification of telomerase activity (TA) in CD-fed mice and EtOH-fed mice. RNase treatment or heat inactivation of KCs isolated from the liver of EtOH-fed mice served as negative controls for the TA assay. All quantitative data are presented as mean ± SD percentage increase compared with CD-fed group (n = 4 in CD-fed group, n = 6 in EtOH-fed group) *P < 0.05, **P < 0.01 vs CD-fed group. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26725521), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Fi, Ha, Pm, Rb, Re, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Fi, Ha, Pm, Rb, Re, Sh

Applications:

, , , , , , , , , , , , , ,

Applications: , , , , , , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-122AF350
Alexa Fluor 405	NB100-122AF405
Alexa Fluor 488	NB100-122AF488
Alexa Fluor 532	NB100-122AF532
Alexa Fluor 594	NB100-122AF594
Alexa Fluor 647	NB100-122AF647
Alexa Fluor 700	NB100-122AF700
Alexa Fluor 750	NB100-122AF750
Allophycocyanin	NB100-122APC
Allophycocyanin/Cy7	NB100-122APCCY7
Biotin	NB100-122B
DyLight 350	NB100-122UV
DyLight 405	NB100-122V
DyLight 488	NB100-122G
DyLight 550	NB100-122R
DyLight 594	NB100-122DL594
DyLight 650	NB100-122C
DyLight 680	NB100-122FR
DyLight 755	NB100-122IR
FITC	NB100-122F
HRP	NB100-122H
Janelia Fluor 549	NB100-122JF549
Janelia Fluor 646	NB100-122JF646
PE	NB100-122PE
PE/Atto594	NB100-122PEATT594
PE/Cy5.5	NB100-122PECY55
PE/Cy7	NB100-122PECY7
PerCP	NB100-122PCP
mFluor Violet 450 SE	NB100-122MFV450
mFluor Violet 500 SE	NB100-122MFV500
mFluor Violet 610 SE	NB100-122MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-122SS

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NB300-221

GAPDH Antibody (1D4)

(19 Reviews)

(411 Publications)

0.1 ml

NB300-221

Analysis of GAPDH in human nucleus pulposus cell culture (40ug/lane) using anti-GAPDH antibody. LI-COR Odyssey imaging system was used for detection. Western blot image submitted by a verified customer review.

Analysis of of HeLa cells stained with GAPDH antibody, dilution 1:100 (Green). DAPI staining of nuclear DNA (Blue). The GAPDH antibody produces strong cytoplasmic staining of healthy cells.

Analysis of cell line lysates probed with mouse mAb to GAPDH (theoretical molecular weight: 36 kDa), NB300-221, dilution 1:2,000: [1] protein standard, [2] HEK293, [3] HeLa, [4] SH-SY5Y, [5] COS1, [6] NIH-3T3, and [7] C6 cells. The GAPDH antibody reveals a single band at ~37 kDa in all cell lines. GAPDH is a house keeping protein, the level of which is relatively unaffected by most experimental manipulations, and, as a result, this antibody has been widely used as a western blotting loading control.

Human eye cell lysate. Antibody used at 1:500. WB image submitted by a verified customer review.

Analysis of GAPDH in chicken pectoralis major using anti-GAPDH antibody. The primary antibody was used at a dilution of 1:4000, incubated for 1 hour at room temperature. Western blot image submitted by a verified customer review.

Application of the approach to other cell lines. The remainder of the protocol from Figure 2 was then applied using 100 ug/mL digitonin as the optimal cytosolic extract in each case. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting and probing with antibodies to GAPDH, BiP and Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). Image collected and cropped by CiteAb from the following publication (//bmcresnotes.biomedcentral.com/articles/10.1186/1756-0500-2-243) licensed under a CC-BY license.

Endothelial responses provoked by Hb-lipid interactions are attenuated by sulfide donors. Confluence HAoECs were exposed to the obtained Hb samples for 8 hours and VCAM-1 expression was determined by Western blotting. GAPDH were used as a loading control. Representative experiment, n = 3. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/omcl/2018/3812568/), licensed under a CC-BY license.

Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 were analyzed in A549 cell treated with NCKU-21 for 24 hr. * P 80% of endogenous Sin1 while levels of myc-FL Sin1 associated with Rictor are comparable with endogenous Sin1 levels. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunodepletions and the effects of RNases and various transcription inhibitors on chromosome condensation and cell cycle state.(A) Western blot for CAP-E, XPB, and Tubulin in Mock or CAP-E depleted extracts. Dilution series of Mock-depleted extracts was used to calculate the % depletion of CAP-E using quantitative fluorescence. (B) 1% agarose gel stained with SYBR safe stain showing RNase A dependent removal of total RNAs from high-speed supernatant egg extracts. (C) Representative fluorescence images of chromatid assembly at steady state (180 min after sperm addition) in the presence of indicated buffers and enzymes. See Materials and methods for details. Note that the high salt in the RNase H buffer causes morphological changes to chromatids regardless of activity. Mean condensation parameters for each condition are indicated in lower left corner of each image. (D) Western blot for XPB and Tubulin in IgG or XPB-depleted extracts. Dilution series of IgG-depleted extracts was used to calculate the % depletion of XPB using quantitative fluorescence. (E) Western blot for XPF, ERCC1, and Tubulin in IgG or ERCC1-depleted extracts. Dilution series of IgG-depleted extracts was used to calculate the % depletion of ERCC1 and XPF using quantitative fluorescence. (F) Representative fluorescence images of chromatid assembly at steady state (180 min after sperm addition) in the presence of DMSO, 30 μM CDK7 inhibitor THZ1, or 30 μM THZ1 and 50 μM triptolide (TPL). (G) Triptolide does not affect CDK1 activation or maintenance of M phase. Western blot for CDK1 T161ph, histone H3T3ph, and Tubulin in M phase HSS extracts in the presence of DMSO or 50 μM triptolide. Both CDK1T161ph (a CDK7 substrate) and H3T3ph are only highly phosphorylated in M phase, and their appearance is not affected by triptolide treatment.Figure 1—figure supplement 1—source data 1.Source data for Figure 1—figure supplement 1A, B,D, E, G.Source data for Figure 1—figure supplement 1A, B,D, E, G. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35293859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Activation of the ATM‐Chk2‐p53 pathway upon CDDP treatmentAConfocal images showing the basal region of organ of Corti cultures treated with either culture medium alone or medium containing 10 μM CDDP for 1 day and immunolabeled for myosin 7A (red) and p‐ATM (green). Scale bar = 15 μm.BHigher magnification images showing representative OHC and IHC nuclei from control and CDDP‐exposed cells. Scale bar = 5 μm.CHistograms displaying green fluorescent signal intensity of x‐projections of OHC and IHC nuclei from control and CDDP‐exposed cells.DQuantification analysis of p‐ATM foci numbers in both OHCs and IHCs exposed to either culture medium alone (light blue and red lines for OHCs and IHCs, respectively) or 10 μM CDDP (blue and red lines for OHCs and IHCs, respectively; n = 50 nuclei per condition and per time point). Data are expressed as mean ± SEM. One‐way ANOVA test followed by post hoc Tukey's test (**P < 0.008, ***P = 0.00005; CDDP‐exposed OHCs versus CDDP‐exposed IHCs).EHigher magnification confocal and 3D images showing the co‐localization of p‐ATM foci (green) with 53BP1 foci (red) in an OHC nucleus from the basal region of the organ of Corti culture treated with 10 μM CDDP for 1 day. Scale bar = 5 μm.FConfocal images showing the basal region of organ of Corti cultures treated with either culture medium alone or medium containing 10 μM CDDP for 1 day and immunolabeled for myosin 7A (red) and p‐Chk2 (green). Scale bar = 15 μm.GHistograms of green fluorescent signal intensity from OHC and IHC nuclei of a CDDP‐treated organ of Corti explant.HQuantification of Chk2‐positive nuclei in both IHCs (red bars) and OHCs (blue bars) from control and CDDP‐treated organ of Corti cultures (n = 50 nuclei per condition and per time point). Data are expressed as mean ± SEM. Kruskal–Wallis test followed by post hoc Dunn's test (*P = 0.045, ***P = 0.0002; CDDP‐exposed IHCs versus control IHCs, CDDP‐exposed OHCs versus control OHCs).IRepresentative Western blots using antibodies against p‐p53 (serine 15), p53, and beta ‐actin in control and 10 μM CDDP‐exposed whole cochlear extracts.J, KHistograms representing the levels of total p53 protein (J) and p53 phosphorylation (K) in control (gray bars) and CDDP‐exposed cochleae (green bars; n = 6 cochleae per condition and per time point). Actin served as a loading control. Data are expressed as mean ± SEM. One‐way ANOVA test followed by post hoc Tukey's test (J: *P ≤ 0.023; K: *P = 0.032, **P = 0.007, ***P ≤ 0.0008; cochleae at the different times after CDDP exposure versus control 12 h).Data information: All experiments were performed in triplicate. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27794029), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

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Reactivity: Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

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NB500-201

Survivin Antibody - BSA Free

(22 Reviews)

(366 Publications)

0.1 ml

NB500-201

<b>Biological Strategies Validation, Genetic Strategies Validation and Orthogonal Strategies Validation.</b>Knockdown Validated: Survivin Antibody [NB500-201] - Western blot analysis using Survivin and flotillin antibodies was performed on lysates of DMSO- and PTX-treated MDAMB231 cells ectopically expressing either control siRNA or Survivin siRNA (panels labeled WCL), as well as on the exosomes these cells generated (panels labeled Exos). Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/8/12/111) licensed under a CC-BY license.

Immunohistochemistry: Survivin Antibody [NB500-201] - Protein expression pattern of Survivin in HCC tissues and non-neoplastic liver parenchyma. IAP members immunoreactivity was estimated by tissue microarray in a subset of HCC patients (n = 40). A-D, Representative Survivin cytoplasmatic immunostaining in a tumor core (A), in a tumor proximal to cirrhosis (C, N: cirrhosis, K: HCC), and in adjacent and long-distance non-neoplastic parenchyma (B and D, respectively). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19397802) licensed under a CC-BY license.

<b>Genetic Strategies Validation. </b>Knockdown Validated: Survivin Antibody [NB500-201] - Anti-tumor effects and functional evidence of sCA-survivin-siRNA in HCT116 and HT29 solid tumor models. Immunostaining of survivin in the tumor tissues on day 19 using [NB500-201]. Scale bar, 50 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0116022) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Survivin Antibody [NB500-201] - Analysis using the HRP conjugate of [NB500-201]. Staining of Telophase with accumulation of survivin in the midbodies of two daughter cells. Survivin detection using [NB500-201].

Western Blot: Survivin Antibody [NB500-201] - Analysis of 30ug of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal [NB500-201] at 1ug/ml. Detection was performed using ECL method with 1 minute exposure. Band detected at higher molecular weight than the predicted MW (16 kDa).

Immunohistochemistry-Paraffin: Survivin Antibody [NB500-201] - Immunohistochemical staining of Survivin in human rectal cancer using [NB500-201] and DAB with hematoxylin counterstain.

Flow Cytometry: Survivin Antibody [NB500-201] - An intracellular stain was performed on HeLa cells with [NB500-201] and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550.

Western Blot: Survivin Antibody [NB500-201] - Western blot analysis using Survivin Antibody [NB500-201]. Effects of siRNA transfection on the expression of Bcl-xL and survivin. Bcl-xL and survivin protein content detected by Western Blotting 48 h after transfection. Bcl-xL and survivin levels are shown normalized to the reference protein beta-actin and relative to the ns-si control. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/6/12297) licensed under a CC-BY license.

Western Blot: Survivin Antibody [NB500-201] - Analysis of Survivin in human hepatocytes from cancer patient (left) and HeLa cell lysate (right) using [NB500-201]. Image from verified customer review. Note: bands detected at higher molecular weight than predicted (16 kDa)

Western Blot: Survivin Antibody [NB500-201] - Western blot analysis using [NB500-201]. Survivin protein is degraded by ubiquitin proteasome in serum-free and serum-containing media. Western blots and protein quantitation graphs showing that addition of MG-132 proteasome inhibitor (10 uM) extended survivin protein half-life in serum-free and serum-containing media. One representative western blot out of triplicate experiments was shown for each treatment and condition. *Indicates the time at which survivin protein is half of the amount at 0 hours (half-life), P < 0.02. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/grp/2012/897678/) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Survivin Antibody [NB500-201] - Analysis of HeLa cells using Survivin Antibody ([NB500-201], 1:10). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).

Immunohistochemistry-Paraffin: Survivin Antibody [NB500-201] - Analysis of Survivin in ovarian cancer tissue using [NB500-201]. Image from verified customer review.

Immunohistochemistry: Survivin Antibody [NB500-201] - HRP conjugated Survivin expression in BIRC5 transfected 293T cells using Survivin Antibody [NB500-201]. Image from verified customer review.

Immunohistochemistry: Survivin Antibody [NB500-201] - Immunohistochemical analysis using [NB500-201]. The top photo is a control stain and the bottom photo is anti-survivin staining of melanoma. Photo courtesy of Dr. Dario Altieri, Yale University.

Immunohistochemistry-Paraffin: Survivin Antibody [NB500-201] - Survivin shows lysates of human neuroblastoma cell line. Polyvinylidene fluoride (PVDF) membrane was probed with 1:200 dilution of 0.5 ug/mL of rabbit polyclonal [NB500-201], followed by 1:2000 dilution of goat anti-rabbit IgG.

Simple Western: Survivin Antibody [NB500-201] - Simple Western analysis using [NB500-201]. Lane view shows a specific band for Survivin in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Theoretical molecular weight: 16 kDa.

Radiation-resistant Caveolin-1 (CAV1)-silenced fibroblasts differentially express and secrete the apoptosis inhibiting protein TP53-regulated inhibitor of apoptosis 1 (TRIAP1).

Expression of survivin protein in cell lines after transfection with siRNA.Survivin protein expression in CHS cell lines was evaluated by western blotting at 48 h after transfection with scrambled and survivin siRNA.

Western blotting analysis in MDA-MB-231 cells and SUM 149 cells.The cells were treated for 24 h with C. juttae essential oil (EO) (46 and 64 μg/ml, respectively). The data shown are the results of a representative experiment.

(A) Levels of suppression of Survivin and expression of p53 for 2 h, 4 h and 8 h for MBA-MD 231 cells. (B) Light microscopy images of the three cell types using nanoconstruct with the AS1411 aptamer. Cell population had been observed to reduce for the MBA-MD 231 cells and AGS while the non-tumorigenic cells MCF-10a did not exhibit any appreciable loss in cell number as well as cell morphology.

Detection of BCL2, Bcl-xL, XIAP and survivin protein content by western blotting 48 h after transfection with a total of 40 nM siRNA in EJ28 bladder cancer cells. Beta-actin was used for loading control.

Effects of siRNA transfection on the expression of Bcl-xL and survivin. (a) Relative mRNA expression levels of Bcl-xL and survivin in EJ28 and J82 bladder cancer cells, 48 h after transfection. Expression values are normalized to the reference gene TBP and are shown relative to the control siRNA

Aurora B phosphorylates EB2.(c,d) HeLa cells were transfected with siRNAs as indicated; after 24 h, the cells were treated with nocodazole for 4 h. Mitotic cells were harvested by mitotic shake-off. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11117), licensed under a CC-BY licence.

Overexpression of Survivin predominantly protects anoikis. B). Caspase-3 activation in EGFP- and EGFP-Survivin-expressing cells after serum starvation under attached or detached culture conditions. The experimental protocol was illustrated in Figure S1. Transfection frequencies were checked by using fluorescence microscopy and confirmed to be 80-90%. Cells were kept in serum-free medium for 24-72 h, harvested, and lysed in Laemmli SDS-sample buffer for immunoblot analysis with anti-GFP, anti-Survivin, anti-activated caspase-3 antibody, anti-LC3B, and anti-alpha-tubulin. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0055710), licensed under a CC-BY licence.

Survivin regulates autophagic flux. (A) U2OS cells stably expressing survivinWTGFP or GFP alone were treated with RAP (200 nM) and CQ (120 uM) for 2 h, then lysed and immunoblotted with anti-LC3, anti-survivin and anti-tubulin antibodies. Immunoblot shown is representative of four independent experiments. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30348810), licensed under a CC-BY licence.

Protein expression pattern of Survivin, XIAP and XAF1 in HCC tissues and non-neoplastic liver parenchyma. IAP members immunoreactivity was estimated by tissue microarray in a subset of HCC patients (n = 40). A-D, Representative Survivin cytoplasmatic immunostaining in a tumor core (A), in a tumor proximal to cirrhosis (C, N: cirrhosis, K: HCC), and in adjacent and long-distance non-neoplastic parenchyma (B and D, respectively). XIAP marked (score 12) and moderate (score 8) immunoreactivity is shown for HCC (E and I, respectively) as well as for cirrhosis (F and L, respectively). G and H, Nuclear XAF1 staining is shown for tumor and non-neoplastic liver whereas XAF1 cytoplasmatic expression in HCC and cirrhosis is shown in panels M and N, respectively. Original magnification x50 and x250, for tissue cores and insets, respectively. Image collected and cropped by CiteAb from the following publication (//bmccancer.biomedcentral.com/articles/10.1186/1471-2407-9-125), licensed under a CC-BY licence.

Survivin and BIM expression in response to lapatinib. Western analysis of Survivin and BIM protein levels after 24 hour exposure to 0.1% DMSO (-) or 2 uM lapatinib (+) in lapatinib-resistant cells (A), cells overexpressing t-Darpp (B), or SK/HerR cells transiently transfected with siRNA targeted to GFP (siCtrl) or Darpp-32/t-Darpp (siDp) for 72 hours (C). alpha-Tubulin was used as a loading control. Protein expression was quantified using ImageJ software. Data was normalized to alpha-Tubulin levels and expressed as the fold change in protein level after lapatinib treatment, relative to the DMSO control, for each cell line. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5311), licensed under a CC-BY licence.

Gene-silencing of Bcl-2, Survivin and XIAP. Western blot showed efficient silencing in transfected MiaPaCa-2 (A) and AsPC-1 cells (B). 50,000 cells/well were single-transfected with carrier solution (lane 1) and siRNA against Luciferase (lane 2) as control. SGS, lowST and ST all effectively silenced the three target genes (lane 3-5). Efficient knock-down was also shown in the lowST group by RT-PCR in MiaPaCa-2 (C) and AsPC-1 cells (D). White bars show controls, grey bars signify transfected cells. All samples were normalized to beta-Actin as a house-keeping gene. SGS = Simultaneous gene silencing; lowST = Low dose siRNA transfection; ST = Standard dose siRNA transfection. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20646298), licensed under a CC-BY licence.

NPC-derived EBNA1 is compromised for interaction with Survivin. F). In situ Proximity Ligation Assay (in situ PLA) is shown for interphase cells from either MUTU-I or C666-1 using mouse anti-EBNA1 and rabbit anti-Survivin. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28077791), licensed under a CC-BY licence.

Survivin is essential for the salinomycin-induced apoptosis in UM cells. A) UM cells were treated with salinomycin for 24 h and the protein levels of apoptosis-related proteins were detected by Western blot. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31718679), licensed under a CC-BY licence.

Pro-apoptotic activity of SAB-13 and SAB-14. (A-C,E,F), FACS analysis of the cells after 48 h treatment. Analysis of apoptosis induction in 22Rv1 (A) and PC-3 cells (B) using Annexin-V-FITC/propidium iodide (PI) double staining. PC-3 cells were pre-treated with 100 uM of pan-caspase inhibitor z-VAD(OMe)-fmk (zVAD) for 1 h and then treated with indicated concentrations of the drugs for 48 h (B). Viable cells (Annexin-V-FITC(-)/PI(-), LL quadrant) or early apoptotic cells (Annexin-V-FITC(+)/PI(-), LR quadrant) were quantified using the Cell Quest Pro software (C) (mean +/- SEM; n = 3; * p < 0.05, Student's t-test). (D) Western blotting analysis of the protein expression in 22Rv1 cells after 48 h of treatment. beta-actin was used as a loading control (mean +/- SEM; n = 3; one-way ANOVA test). Anisomycin (Aniso; treatment with 10 uM for 48 h) was used as a positive control. (E,F) Cell cycle analysis of 22Rv1 cells using PI staining, apoptotic cells were detected as sub-G1 population (E) (mean +/- SEM; n = 3; * p < 0.05, one-way ANOVA test). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32403427), licensed under a CC-BY licence.

Short‐term nicotine exposure does not alter Lypd6, Lynx1, or Ly6H levels in the brain. Lypd6, Lynx1, Ly6H, and beta 2 nAChR subunit protein levels were analyzed in (a) frontal cortex (FC) and hippocampal (HIP) tissue from rats administered nicotine (0.4 mg/kg s.c., twice daily) or vehicle (0.9% saline) for 7 days from day 8–14 or (b) 54–60 (n = 8). (c and d) Representative images of western blots summarized in (a) and (b), respectively. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27344019), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$UroA/UAS03 enhance tight junction proteins in AhR-dependent manner. a HT29 cells were treated with vehicle (DMSO-0.01%)/UroA/UAS03 (50 μM) for 24 h. mRNA levels of Cytochrome P450 1A1 (Cyp1A1) was measured by RT PCR. b Cyp1A1 protein levels were measured using immunoblots and quantified band intensities by Image J software. c Cyp1A1 enzyme activity was measured by P450-Glo Cyp1A1 assay. HT29 cells were treated with UroA or UAS03 (0.1, 1, 10, 25, 50 µM) or FICZ (0.1, 1, 10, 25, 50 nM) for 24 h and enzyme Cyp1A1 activity was measured. d C57BL/6 and AhR−/− (n = 3) mice were treated orally with Vehicle (0.25% CMC), UroA or UAS03 (20 mg/kg) for 1 week and Cyp1A1 activity was measured in colons and livers by ethoxyresorufin-O-deethylase (EROD) assay. e The cells expressing AhR-reporter (luciferase) were treated with Veh or UroA/UAS03 or ellagic acid (EA) or MeBio (AhR high affinity ligand) for 6 h and fold change of luminescence over vehicle treatment was measured. f Immunofluorescence confocal images of HT29 cells treated with vehicle/UroA/UAS03 (50 μM) for 6 h. The cells were stained with anti-AhR antibody (red) and DAPI (blue). Relative fluorescence (n = ~20 cells) in the cytosol and nucleus was measured. The scale bar indicates 10 μm. g AhR levels in cytosol and nuclear fractions of HT29 cells treated for 2 h with Veh or UroA/UAS03 (50 μM). h AhR or i Cyp1A1 was knocked down using siRNA in HT29 cells and the cells were treated with vehicle/UroA/UAS03 (50 μM) for 24 h and immnunoblots were performed to detect expression of AhR, Cyp1A1, and Cldn4. Scrambled (Sc) siRNA transfections were used as controls. Immunoblots were quantified using Image J software. The data is representative of two independent repeats with triplicate wells for each treatment. Statistics performed using unpaired t-test using Graphpad Prism software. All in vitro studies were performed in triplicates. Error bars, ±SEM; ***p < 0.001; **p < 0.01; **p < 0.05. Source Data are provided as a Source Data File Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30626868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Characterization of MSCmix and NCSCmix isolated from the bone marrow of adult Wnt1-CRE/R26R-LacZ mice. After recombination, NCSCs from Wnt1-CRE/R26R-LacZ mice express LacZ gene. MSCs did not undergo Cre/Lox recombination and conserved the PGK-Neo cassette (a). MSCmix are adherent fibroblast-like cells, do not express beta -galactosidase (b) or Sox2 c (red), slightly express Nestin (c) (green), p75NTR (d) (red), and Sca-1 (d) (green). NCSCmix have a similar morphology, express beta -galactosidase (e), Nestin (f) (green), Sox2 (f) (red) and p75NTR (g) red), but not Sca-1(g) (green). Scale bar = 20 μm. MSC mesenchymal stem cell, NCSC neural crest stem cell Image collected and cropped by CiteAb from the following open publication (//stemcellres.biomedcentral.com/articles/10.1186/s13287-015-0202-2), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Aryl hydrocarbon receptor interacting protein (AIP) immunostaining.A and B—Examples of low AIP expression; C and D: Examples of high AIP expression; E—Normal human pituitary staining with omitting primary antibody (negative control); F—Normal human pituitary staining with AIP (positive control); Scale bar = 1000 μm. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0117107), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Repression of p21 by APE1 in p53-null cells and effect of ectopic p53 in this repression.(A & B) Real Time RT-PCR analysis showing relative quantitation of p21 transcript level in (A) HCT116p53null cells with WT and N delta 42 APE1 overexpression; *: p value (n = 4) calculated from control (empty vector transfection) vs. WT or N delta 42 APE1 overexpression, and (B) control (control siRNA) vs. APE1-depleted HCT116p53null cells; *: p value <0.05 (n = 4) calculated from control vs. APE1-depleted cells. (C) Effect of ectopic p53 expression on p21 transcript level in control vs. APE1-depleted HCT116p53null cells. First, cells were transfected with control siRNA or APE1 siRNA, the next day both the cell types were again transfected with empty vector or p53 expression vector and after 48 hrs the cells were harvested; signal from empty vector transfection in both control and APE1-depleted cells were set as reference samples; *: p value <0.05 (n = 3) calculated based on the effect of ectopic p53 expression over empty vector transfection in control vs. APE1-depleted cells. (D) Effect of APE1 depletion in control (empty vector transfected) vs. ectopic p53-expressing HCT116p53null cells; the same experiment was performed as in C but analyzed differently; signal from control siRNA-transfected cells in both empty vector transfected and ectopic p53 expressing cases were set as reference samples; *: p value <0.05 (n = 3) calculated based on the effect of APE1-depletion in empty vector transfected vs. ectopic p53 expressing cells. (E) Representative Western analysis of p53, APE1, p21 and alpha -Tubulin levels in the same HCT116p53null cells as in B–D. (F & G) Real Time RT-PCR analysis of p21 level in Saos2 cells as in C & D. *: p value <0.05 (n = 2). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23874636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Pre-treatment with 0.5 mM sodium arsenite (SA) enhances permissivity in a cell-type-specific manner across reovirus strains. (A) CV-1, HeLa, L929, or HPDE cells were left untreated (no SA) or were treated with 0.5 mM SA for 30 min prior to infection (Pre-SA). Following this, cells were infected with T3D such that ~20% to 50% of cells were infected and at 18 h p.i. cells were fixed and immunostained for μNS and DAPI to visualize viral factories (VFs). The percent of cells containing VFs was quantified ((# of cells containing VFs/total # of cells) × 100) from three independent experiments. The expression level of μNS (B) and μ1 (C) was determined in CV-1, L929, or HeLa cells either left untreated (no SA) or treated with 0.5 mM SA for 30 min (Pre-SA) before infection with T3D at MOI = 1. At 18 h p.i., cells were harvested and the expression level of the indicated proteins was determined by immunoblot. M = mock. Densitometry analysis of the band intensity for μNS and μ1 was adjusted to the matched alpha -tubulin loading control for two independent experiments. Columns represent mean ± SEM. (D) CV-1; (E) L929; or (F) HeLa cells were left untreated (no SA) or were treated with 0.5 mM SA prior to infection (Pre-SA). Cells were then infected with the reovirus strains, T3D, T1L, or T3A, as described in (A). At 18 h p.i., cells were fixed and immunostained for μNS and DAPI to detect VFs. The percent of cells containing VFs was quantified ((# of cells containing VFs/total # of cells) × 100) from at least two independent experiments. * p < 0.05; ** p < 0.01; two-tailed unpaired t test. The error bars indicate S.D. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31216693), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Inhibition of Rac1 by N17Rac1 mutant or Rac1 siRNA diminishes IR-induced G2/M checkpoint activation. (A) MCF-7 cells were infected with Ad.N17Rac1 or Ad.Control for 24 hours and exposed to 15-Gy IR. Left panel: the cells were analyzed for DNA content 24 hours after IR. The result depicts the percentage of cells with 4N-DNA content and is shown as mean ± SD of quadruplicate samples. *P < 0.001 (n = 4), significant difference from the irradiated Ad.Control-infected cells. Right panel: Inset: at 15 minutes after IR, the infected cells were analyzed for Rac1 activities (Rac1-GTP) and protein levels (total Rac1). Bar graph: mitotic cells in the cell samples were analyzed 2 hours after IR. The result depicts the percentage of mitotic cells and is shown as mean ± SD of triplicate samples. **P = 0.002 (n = 3), significant difference from the irradiated Ad.Control-infected cells. (B) Upper panel: MCF-7 cells transfected with Rac1 siRNA (Rac1) or control siRNA (Control) were incubated for the indicated times and analyzed for protein levels of Rac1 and Actin. Lower panel: After 2-day incubation, the siRNA-transfected cells were exposed to IR, incubated for 24 hours, and assessed for DNA content. Results depict the percentage of cells with 4N-DNA content and represent the mean ± SD of three separate experiments in duplicate samples. *P < 0.001 (n = 6), significant difference from the irradiated Control-siRNA transfected cells. (C) After 2-day incubation, siRNA-transfected cells were treated with/without 20-Gy IR, incubated for 1 hour, and analyzed for ATM, ATR, Chk1, and Chk2 activities. Image collected and cropped by CiteAb from the following open publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Myocardial infarction (MI) increased TLR3 expression and its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) and (B) show mRNA and protein levels of TLR3 in sham and MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE and immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 and Trif, but not MyD88, was detectable in sham myocardium and was increased in infarct myocardium. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Vps13 co-fractionates with Rab7 and Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic and membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker and GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble and insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) and the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) and ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 and Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Ca, Fe, Gp, Ha

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Fe, Gp, Ha

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB500-201AF350
Alexa Fluor 405	NB500-201AF405
Alexa Fluor 488	NB500-201AF488
Alexa Fluor 532	NB500-201AF532
Alexa Fluor 594	NB500-201AF594
Alexa Fluor 647	NB500-201AF647
Alexa Fluor 700	NB500-201AF700
Alexa Fluor 750	NB500-201AF750
Allophycocyanin	NB500-201APC
Biotin	NB500-201B-0.1ml
DyLight 350	NB500-201UV
DyLight 405	NB500-201V-0.1ml
DyLight 488	NB500-201G-0.1ml
DyLight 550	NB500-201R-0.1ml
DyLight 594	NB500-201DL594
DyLight 650	NB500-201C-0.1ml
DyLight 680	NB500-201FR
DyLight 755	NB500-201IR
FITC	NB500-201F-0.1ml
HRP	NB500-201H-0.1ml
Janelia Fluor 549	NB500-201JF549
Janelia Fluor 646	NB500-201JF646
PE	NB500-201PE
PerCP	NB500-201PCP
mFluor Violet 450 SE	NB500-201MFV450
mFluor Violet 500 SE	NB500-201MFV500
mFluor Violet 610 SE	NB500-201MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB500-201SS

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NB100-2323

IRE1 alpha [p Ser724] Antibody - BSA Free

(9 Reviews)

(318 Publications)

0.1 ml

NB100-2323

P-Ire1a activation correlates with WFS1 cell expression. Cryosections of retina from 12 month old Wfs1+/+ and Wfs1-/- mouse were immunostained with anti-P-Ire1a antibody (red). DAPI was used for staining of cell nuclei (blue). RPE, retinal pigment epithelium; ONL, outer nuclear layer; INL, inner nuclear layer, RGC, retinal ganglion cells. Scale bars=50 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0097222) licensed under a CC-BY license.

Hepatic ER stress markers with cachexia progression. ER stress markers Bip, IRE1a, ATF6p50 and CHOP were examined in the liver of non, pre and severely cachectic mice. (n = 6-8 per group, p < 0.05) Dotted line indicates levels of Non-cachectic mice. Non = Non-Cachectic Apc Min/+ Sev = severely cachectic Apc Min/+; * denotes significantly different from Non-cachectic Apc Min/+ Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0119888) licensed under a CC-BY license.

IRF-1 plays a central role in ER stress-mediated modulation of VCAM-1 expression by TGRL. HAEC were conditioned for 4 hr with TNFa (0.3 ng/ml) E: CHOP knockdown decreased TNFa-induced VCAM-1 expression. n=4. **P<0.01 vs. siCtrl+TNFa. Shown are representative blots from 3 independent experiments with similar results. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0078322) licensed under a CC-BY license.

Analysis using HRP conjugate of NB100-2323. Detection of phosphorylated IRE-1 alpha using NB100-2323. Lane 1: COS-7 untransfected Lane 2: COS-7 expressing wild-type IRE1 alpha Lane 3: COS-7 expressing kinase-dead IRE1 alpha. Theoretical molecular weight: 110 kDa.

<b>Biological Strategies Validation. </b>Analysis of anti-IRE1 alpha (pSer724) using Lot AN and AO of NB100-2323. HeLa cells were treated (+) or untreated (-) with 10 mM DTT for 60 min to activate the UPR. Total protein was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% BSA in TBST. The membrane was probed with 2.0 ug/ml antibody in 5% BSA, and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Theoretical molecular weight: 110 kDa.

Regulation of the unfolded protein response by KLF15. Western analysis of UPR activity in WT versus KLF15-/- primary hepatocytes. Hepatocytes were isolated from standard chow-fed 4-month-old male WT and KLF15 -/- mice. Two individual experiments were performed in triplicate; each lane indicates a technical replicate. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0077851) licensed under a CC-BY license.

HeLa cell lysate, 20 ug. Antibody at 1:1000, 1% skim milk in TBST, overnight incubation at 4C. WB image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Detection in Min6 cells which were treated with different concentrations of glucose for 3 hours prior to lysates preparation.

IRE1 (pS724) was detected in immersion fixed paraffin-embedded sections of human spleen using Rabbit Anti-Human IRE1 (pS724) polyclonal Antibody (Catalog # NB100-2323) at 1:300 for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the perinuclear cytoplasm in splenocytes.

Hepatic ER Stress.Representative hepatic western blots of BiP, phosphorylated (Ser51), total EIF2 alpha and phosphorylated:total EIF2 alpha , phosphorylated (Ser724), total IRE1 alpha and phosphorylated:total IRE1 alpha , and CHOP (n = 9). Diets not sharing a common letter differ significantly from one another (P≤.05).

Morphine suppressed 6-OHDA-induced ER stress through activation of UPR. (A,B) Morphine induced UPR in SH-SY5Y cells. Protein levels of GRP78, p-IRE1 alpha , IRE1 alpha , p-PERK, PERK, ATF6, CHOP and Tubulin in SH-SY5Y cells were analyzed (A) and quantified (B) by western blot. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001 vs. control.

Effect of cancer on ER stress markers.Bip1, IRE-1, ATF-6 p50 and CHOP expression in the liver of non—cachectic ApcMin/+ mice (N = 6 per group), compared to healthy C57BL/6 mice. Dotted line on the western blot indicates two different sections of the same gel. Values are expressed as Mean ± SE. * denotes significantly different from the healthy C57BL/6 mice as analyzed by a pre—planned t—test. p < 0.05.

T helper cells upregulate the IRE1a-XBP1 pathway during activation. c) Naive T helper cells and in vitro differentiated Th2 lymphocytes were analyzed for IRE1a mRNA expression by qRT-PCR (left panel), protein expression by Western blot (middle panel), and phosphorylated IRE1a (P-IRE1a) by Western blot (right panel). The density of Western blot bands from five independent experiments of IRE1a and three independent experiments of phospho-IRE1a were measured and displayed on top of each Western blot panel. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30355343), licensed under a CC-BY licence.

IER3IP1 suppression decreases the UPR activation. (B) Effect of IER3IP1 suppression on the IRE1alpha arm of the UPR. 4 days after IER3IP1 KD in MIN6 cells, phosphorylation of IRE1alpha, Bip, sXBP-1 and uXBP-were determined by Western blot. The loaded proteins in the two

CETP inhibition reduces endoplasmic reticulum stress. HAECs transfected with CETP or control scrambled siRNA. (B) Phosphorylated and total IRE (n = 3, ns). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33430172), licensed under a CC-BY licence.

Apoptosis mediated by Arl6ip5 interference is regulated by Chop. (a) Immunoblotting was used to detect the protein level for p-IRE1alpha, IRE1, Chop, Arl6ip5 and beta-actin in the UAMS-32 cell with NC-siRNA or Arl6ip5-siRNA treatment for 72 h. Representative results were shown from three independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014427), licensed under a CC-BY licence.

Activation of UPR signaling pathways after UIRI. e and f) The expression of p-IRE1 and t-IRE1 in mice kidneys were evaluated with western blotting and quantified. Data are expressed as means +/- SEM, n = 3 ~ 6 in each group. *P < 0.05, **P < 0.01, and ***P < 0.001, as compared with sham group Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35765067), licensed under a CC-BY licence.

Effect of Insig-1 overexpression on nSREBP-1c and proteins related to ER stress pathway in INS-1 cells. INS-1 and INS-1-Insig-1 cells were stimulated with 11.2 mM and 25.0 mM glucose for 0, 24 and 72 h. A) nSREBP-1c and p-IRE1alpha pathway of ER stress related proteins were detected by Western blot. GAPDH was used as control for protein loading. Equal amount of proteins (50 ug) were loaded. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21843373), licensed under a CC-BY licence.

Protein expression of downstream markers of ER stress in islets from lean, obese and high-fat-diet-fed fZDF rats. Protein lysates from islets isolated from three age-matched fZDF rats (obese), HF-fZDF (HFD) rats and their heterozygous lean littermates (lean) were separated by SDS-PAGE and analysed by western blotting. As controls, lysates from the islets isolated from Wistar rats or MIN6 cells treated with 1 uM thapsigargin for 2 h or sorbitol for 1 h were run alongside. Proteins were detected using antisera against (a) Calreticulin, HYOU1, GRP78, p-IRE1alpha, p-eIF2alpha and CHOP and as protein loading control rpS6 and (b) p-JNK and total JNK1/2 as loading control. Western blots were quantified using Image-J software. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/nutd201335), licensed under a CC-BY licence.

ABT-263 induces ER stress and activation of the unfolded protein response. c) Kinetic analysis of ER stress proteins in Mel270 cells treated with ABT-263 5 uM in the absence or presence of qVD-OPh 20 uM. HSP90 is used as a loading control. Representative western blots are shown. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32337074), licensed under a CC-BY licence.

$Localization of the WT and mutant Wrn proteins in different subcellular fractions. (C) Protein levels of GRP78, phosphorylated IREalpha, and beta-actin (top panels) and of total IREalpha, and beta-actin (bottom panels) in the spleen of three animals of each genotype. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26447695), licensed under a CC-BY licence.$

Glucocorticoids suppress NIX expression independent from PINK1-parkin pathway.a SH-SY5Y cells were incubated with cortisol for 12 h and mRNA expressions were analyzed by real-time PCR. n = 5. b, c Hippocampal neurons and SH-SY5Y cells were treated with corticosterone for 24 h and with cortisol for various time, respectively. Expression of NIX, PTEN-induced kinase 1 (PINK1), and BCL2 interacting protein 3 (BNIP3) were detected via western blot. n = 5. d, e Hippocampal neurons and SH-SY5Y cells were treated with corticosterone and cortisol, respectively, for 24 h. NIX (green), TOMM20 (red), and DAPI (nuclear counterstaining, blue) were visualized. Scale bars, 20 μm (magnification, ×1000). n = 5. f Nontargeting (NT) or PARK2 siRNA was transfected to SH-SY5Y cells for 24 prior to cortisol for 24 h. NIX was co-immunoprecipitated with parkin. Parkin levels in immunoprecipitated samples were quantified. n = 5. g, h Both hippocampal neurons and SH-SY5Y cells were transfected with mitochondria-targeted Keima (mt-Keima)-Red-Parkin for 24 h prior to corticosterone and cortisol for 24 h, respectively. Western blot was performed. n = 5. i–l Both hippocampal neurons and SH-SY5Y cells were pretreated with phorbol 12-myristate 13-acetate (PMA, 10 nM) for 30 min before corticosterone and cortisol for 24 h, respectively. i, j Hippocampal neurons and SH-SY5Y cells were transfected with mt-Keima at DIV 5 and 48 h prior to treatment, respectively. DAPI was used for nuclear counterstaining (blue). Ratio of red to sum of red and green was quantified. Scale bars, 20 μm (magnification, ×1000). n = 5. k, l TOMM20 levels were detected by western blot. n = 5. m SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/NIX-c-eGFP vector for 24 h prior to cortisol for 24 h. TOMM20 levels were detected by western blot. n = 5. All blots and immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. The representative images were acquired by SRRF imaging. Two-sided unpaired student’s t test: Figs. 3a, b, d, e. Two-sided one-way ANOVA: Fig. 3c. Two-sided two-way ANOVA: Figs. 3f–m. ** indicates p < 0.01 versus control. ## indicates p < 0.01 versus corticosterone in hippocampal neurons and cortisol in SH-SY5Y. Data are provided as a Source data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Expression analysis of mouse Fchsd1 and Fchsd2 in different tissues.(A) Total RNA from postnatal day 5 mouse tissues was extracted and used as template for reverse transcription. PCR was performed using this cDNA as template. Upper panel, Fchsd1 mRNA is expressed more abundantly in nervous tissues. Middle panel, Fchsd2 mRNA is expressed ubiquitously in all tissues examined. Lower panel, beta -actin specific primers were used as the RT-PCR template control. (B) Total proteins of postnatal day 5 mouse cochlea and vestibula were extracted and separated by PAGE and detected with antibodies against FCHSD1(Novus), FCHSD2, or SNX9. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23437151), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LAIR-1 inhibits Glut1-related glucose uptake in OS cells. a Heatmap showing the levels of differentially expressed mRNAs. b Top 20 KEGG pathway annotation categories for target gene functions of predicted mRNAs. c Selected significantly differentially expressed mRNA-related to EMT in RNA-seq data between two groups, ***P < 0.001. d qPCR validation of differentially expressed EMT-related genes in LV-NC and LV-LAIR-1-overexpressing OS cells, **P < 0.01. e Glut1 expression analyzed by western blotting. f Immunofluorescence staining of Glut1 in the LV-LAIR-1-overexpressing OS cells. Scale bar = 50 μm. Data were obtained from at least two independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32563267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Phase contrast microscopy images of HFA and brain tumor cells and immunofluorescence images of cultured primary brain tumor cells, AA and HFA.HFA were derived from three different foetal brains. (A) 18-week foetus (10× magnification); (B) 19-week foetus, first week in culture (10× magnification); (C) 19-week foetus, day 5 in culture (20× magnification); (D) Primary GBM after 2 trypsinisations (20x); (E) Recurrent GBM (20x); (F) Secondary GBM after 3 trypsinisations (10x); (G) OII 14 days in culture (10x); (H) AII 13 days in culture (10x); (I) Negative control for NGS merged with DAPI; (J) Negative control for secondary antibodies merged with DAPI; (K) GBM cells derived from one patient – GFAP (DAKO) merged with DAPI and CD68 (zoomed: 2.4× magnification); (L) primary brain tumor cells from one patient (male, 40 years old) (passaged three times) - GFAP (Novocastra) merged with DAPI; (K and L) GFAP (green) was used as a GBM marker and CD68 (red) was used as a marker for microglia. (M) AA from one Female, 61 years old; (passaged twice) - GFAP (Novocastra) merged with DAPI; (N) AA from one male 40 years old; (passaged once) - GFAP (Sigma) merged with DAPI and CD68 (Abcam); (M and N) GFAP (green) was used as an astrocyte marker and CD68 (red) and CD11b (green) were used as markers for microglia; (O) HFA from one 17-week- old foetus (passaged once) - GFAP (Novocastra) merged with DAPI and CD11b (Novus); (P) HFA from an 18-week- old foetus (passaged once) - GFAP (DAKO) merged with DAPI and CD68 (zoomed: 2.1× magnification); (O and P) GFAP (green and red) was used as an astrocyte marker and CD68 (red) and CD11b (green) were used as markers for microglia. Nuclei indicated by DAPI (blue) in all images. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0112945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Regulation of FOXC1 on TLR3/4 expression in mice subjected to myocardial ischaemia (MI). The siRNA against FOXC1 (si‐FOXC1) or FOXC1 adenovirus (Ad‐FOXC1) was injected into the left ventricle just after LAD ligation to generate FOXC1 knockdown (A) or FOXC1 overexpression (B), and the negative control (NC) siRNA and Ad‐GFP served as control, respectively. The mRNA (upper panel) and protein (middle and lower panel) levels of TLR3/4 were determined after 2 wk. Data are means ± SEM aP < .05, AP < .01 vs respective MI Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31517441), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Analysis of protein levels of genes with increased transcription in hypoxia, IOX2 and VH032.HIF targets were increased in hypoxia, VH298 and FG-4592. 0.05% DMSO (vehicle control), 1% O2 (hypoxia), 100 µM VH298 and 50 µM FG-4592 were introduced to (A) HeLa or HFF for 24 hours and (B) HeLa for indicated time. Protein levels were analysed by immunoblotting using antibodies against indicated proteins, with beta -Actin as loading control. The blots shown are representative of three independent experiments. * indicates longer exposure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30801039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Dr, Gt, Ma, Pm, Pm, Rb, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Dr, Gt, Ma, Pm, Pm, Rb, SyHa

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-2323AF350
Alexa Fluor 405	NB100-2323AF405
Alexa Fluor 488	NB100-2323AF488
Alexa Fluor 532	NB100-2323AF532
Alexa Fluor 594	NB100-2323AF594
Alexa Fluor 647	NB100-2323AF647
Alexa Fluor 700	NB100-2323AF700
Alexa Fluor 750	NB100-2323AF750
Allophycocyanin	NB100-2323APC
Biotin	NB100-2323B
DyLight 350	NB100-2323UV
DyLight 405	NB100-2323V
DyLight 488	NB100-2323G
DyLight 550	NB100-2323R
DyLight 594	NB100-2323DL594
DyLight 650	NB100-2323C
DyLight 680	NB100-2323FR
DyLight 755	NB100-2323IR
FITC	NB100-2323F
HRP	NB100-2323H
Janelia Fluor 549	NB100-2323JF549
Janelia Fluor 646	NB100-2323JF646
PE	NB100-2323PE
PerCP	NB100-2323PCP
mFluor Violet 450 SE	NB100-2323MFV450
mFluor Violet 500 SE	NB100-2323MFV500
mFluor Violet 610 SE	NB100-2323MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-2323SS

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NB110-53818

ATG5 Antibody - BSA Free

(7 Reviews)

(266 Publications)

0.1 ml

NB110-53818

CQ increased CDDP-induced cell death in drug-resistant EOC through autophagy inhibition and induction of p21WAF1/CIP1.a A2780-CP20 cells stably expressing control or ATG5 shRNA were treated with CDDP for 48 h, and the expression of ATG5 and autophagy marker proteins, LC3 and p62, were analyzed by western blot using specific antibodies. Knockdown efficiency of ATG5 was shown by western blot. Expression of LC3 and p62 was also analyzed by western blot in A2780-CP20 cells treated with CDDP, CQ, or the CQ-CDDP combination for 48 h. beta-actin was used for a protein-loading control. shRNA/CP20 represents control-shRNA- or ATG5-shRNA-expressing A2780-CP20 cells. Western blot was performed three times, and representative data are presented (left panel). The amounts of p62 and LC3-I and -II normalized to the amount of beta-actin are represented by a bar graph (middle and right panels, respectively). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33277461), licensed under a CC-BY licence.

FIGURE 2: Blockage of autophagy leads to increased plp mRNA and protein levels. (B) Western blot analysis with antibodies against Atg5, P62, PLP and MBP proteins in optic nerve lysates of 6mo control and cKO mice. Representative images of a single experiment are depicted. Image collected and cropped by CiteAb from the following publication (//www.cell-stress.com/researcharticles/2022a-ktena-cell-stress/), licensed under a CC-BY licence.

LHPP suppresses aerobic glycolysis.A Relative mRNA expression levels of glycolytic genes and glutamine transporters in LHPP-overexpressing or LHPP-knockdown MGC-803 cells and control cells by qPCR. B Protein expression levels of glycolytic genes and glutamine transporters in LHPP-overexpressing or LHPP-knockdown MGC-803 cells and control cells on western blot. C IHC staining of LHPP and HIF1A in TMAs and their correlation. Scale bars = 100 μm. D Oxygen consumption rate and extracellular acidification rate of LHPP-overexpressing or LHPP-knockdown MGC-803 cells and control cells were measured using the Seahorse Bioscience XF96 analyser. E Human phosphokinase microarray assay analysis of the conditioned medium from stably transfected HGC-27 cells. A summary of the relative signal intensities of the indicated proteins is shown. G, H IHC staining of LHPP and p-GSK3b in TMAs and their correlation. Scale bars = 200 μm. F Combined LHPP and GSK3b by co-immunoprecipitation. I Protein expression levels of the Wnt pathway in LHPP-overexpressing or LHPP-knockdown MGC-803 cells and control cells on western blot. Data were analyzed using the Wilcoxon test. *P < 0.05, **P < 0.01, ***P < 0.001, KEGG Kyoto encyclopaedia of genes and genomes, GO gene ontology, qPCR quantitative polymerase chain reaction, IHC immunohistochemical, TMA tissue microarray. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35568711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

WNT11 is induced by hypoxia or hypoxic mimetics in different cell types.(A) Increased Wnt11 mRNA in EMSC adipocytes (Day 12) after hypoxia-mimetic treatments. EMSC adipocytes were treated with CoCl2 (0.1 mM), DFO (0.1 mM) or DMOG (0.1 mM) for 24 hrs. Values were normalized to Tbp mRNA and are expressed relative to control (n = 3). (B,C) Increased Wnt11 mRNA by hypoxia in EMSC preadipocytes and adipocytes (Day 0–12 after differentiation) (B), and C2C12 myoblast and myocyte (Day 0 and 8 after differentiation) (C). Wnt11 mRNA was assessed by quantitative PCR in cells exposed to air (21% O2) or hypoxia (1% O2) for 24 hrs. (n = 4). Values were normalized to Tbp mRNA and are expressed relative to 21% O2 samples (left panel). (D) Immunoblot analyses of HeLa cells under normal air or hypoxia for 24 hrs. (E,F) Induction of Wnt11 by increasing concentrations of DMOG in MDA-MB-231 cells (E) and 4T1 cells (F). (G) EMSCs treated with 0.1 mM DMOG for the indicated times. Wnt11 and Vegf mRNA expression was measured by qPCR and normalized to Tbp mRNA (n = 4). (H) WNT11 protein levels after DMOG treatment normalized to alpha -Tubulin (upper panel; n = 4). Representative immunoblots of EMSCs treated with 0.1 mM DMOG for the indicated times (Lower panel). (I) Protein expression in MDA-MB-231 cells treated with 0.1 mM DMOG. (J) Induction of Wnt11 promoter activity by hypoxia or hypoxia mimetics. pGL3-Wnt11 promoter plasmid was transfected into C2C12 cells. Cells were incubated with DMOG (left panel, n = 4) or under 21% O2 or 1% O2 (right panel, n = 8) for 24 hrs. For panels (A–C,G,H,J), values are mean ± s.e.m. *p < 0.05, **p < 0.01. For panels of immunoblotting, laminin, alpha -tubulin, and ERK were used as loading controls, WNT11 normalized to alpha -Tubulin was shown. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep21520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Representative microscopy images of staining for hypoxia markers in prostate tissues (MO, 400×). A) HIF-1 alpha - notice the granular cytoplasmic immunoreactivity of the malignant epithelial cells. In this case, more than 50% of the glands stained. B) LOX - strong and diffuse nuclear immunoreactivity of the epithelial cells. C) CAIX - note a focal apical cytoplasmic immunoreactivity in epithelial cells. D) VEGFR2 - moderate nuclear and weak cytoplasmic expression of the epithelial cells Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28143503), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Interaction of Nesprin-2-SMC and Nesprin-2 with SMC2 and SMC4. (a) Precipitation of SMC2 and SMC4 with GST-Nesprin-2-SMC from HaCaT cell lysates. Precipitates were resolved on SDS-polyacrylamide gels (10% acrylamide) and probed with SMC2 and SMC4 specific antibodies. SPN, supernatant after pulldown; PD, pulldown. The lower molecular weight band in the SMC2 pulldown is presumably a breakdown product. (b) Immunoprecipitation of SMC2 from HaCaT cell lysates with Nesprin-2 specific mAbK20-478 and of Nesprin-2 with SMC2 specific antibodies. GFP-specific monoclonal antibodies were used for control. The antibodies used for immunoprecipitation are indicated above the panels (IP). The blots were probed with the antibodies listed on the right (WB). Immunoprecipitates were resolved on gradient gels (3–12% acrylamide) and 10% acrylamide gels as appropriate. The data are from one blot; however, the input was not directly adjacent to the SMC2 IP. (c) Interaction of CAP-H2 (condensin II) and CAP-H (condensin I) with Nesprin-2-SMC. Pulldowns were performed with HaCaT cell lysates and GST for control and GST-Nesprin-2-SMC as indicated. Unsynchronized cells were used for the experiments shown in (a)–(c). (d) Analysis of the Nesprin-2-SMC interaction with SMC2 during the cell cycle. HaCaT cells were synchronized with RO-3306 or other reagents as described in Materials and Methods in order to obtain the relevant cell cycle phases. Cell cycle phases were assessed by FACS analysis; the results are depicted in the accompanying diagram. Pulldown was carried out with GST-Nesprin-2-SMC bound to GST-Sepharose. GST was used for control. The blot was probed with SMC2 specific antibodies. (e) Localization of Nesprin-2 as detected with mAb K81-116-6 (green) during mitosis in HaCaT cells. DNA was stained with DAPI. Arrow points to filamentous staining across the chromosomes. (f) Nesprin-2 distribution in HaCaT cells during mitosis as detected with mAb K20-478 (green) and pAbK1 (red). DNA was detected with DAPI. Bar, 10 μm. (g) Nesprin-2 presence on chromosomes. Different Z-stacks (from top to bottom: 0 μm, 0.21 μm 0.42 μm, and 0.84 μm) from a COS7 cell in anaphase stained with mAb K20-478. DNA was stained with DAPI. Bar, 5 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29445399), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Representative human colorectal cancer specimen. Immunohistochemistry of CA9 and GGT1 in mLNs. In these cases, both CA9 and GGT1 were expressed, suggesting that GGT1 expression is related to hypoxia in mLNs. Scale bar, 500 μm. Black arrowheads: GGT of cancer cells, white arrowheads: GGT surrounding cancer cells, arrow: accumulation of GGT. mLNs: metastatic lymph nodes, GGT: gamma-glutamyl transpeptidase. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30542087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Modulation of A152T-tau clearance and pathology by upregulation of autophagy. (A and B) Treatment of A152T-tau fish with the autophagy inducers clonidine (A), rapamycin or rilmenidine (B), accelerated clearance kinetics of A152T-tau (mean ± SD of n ≥ 40 neurons/group; Student-Newman-Keuls one-way ANOVA, */#P < 0.05; **/##P < 0.01 ***P < 0.001 versus untreated). (C) Treatment with rapamycin (rap), clonidine (clo) or rilmenidine (ril) also ameliorated morphological defects in A152T-tau transgenic fish (n = 6 independent experiments, 20 fish/group, mean ± SD; Student-Newman-Keuls one-way ANOVA, *P < 0.05; **P < 0.01 and ***P < 0.001 versus DMSO). (D) Representative image showing rapamycin treatment reduced the proportion of abnormal A152T-tau fish. Scale bar = 3.5 mm. (E) Quantification of the escape response measured in individual A152T-tau fish 3 dpf, treated with either DMSO, rapamycin, clonidine or rilmenidine. (n = 5 independent experiments in triplicate, 15/group shown as mean ± SD; two-tailed t-test: *P < 0.05, **P < 0.01 and ***P < 0.001 versus DMSO). The treatment with autophagy upregulators improved the escape response deficit in A152T-tau fish. (F and G) Induction of autophagy by the addition of rapamycin or rilmenidine to A152T-tau fish also reduced levels of phosphorylated tau at residues Ser202/Thr205 (AT8) and Ser396/Ser404 (PHF1) relative to total tau levels (n = 3 independent experiments in duplicate, 10/group shown as mean ± SEM; two-tailed t-test: *P < 0.05 and ***P < 0.001 versus DMSO). (H and I) Treatment with autophagy upregulators results in less cell death. Rilmenidine treatment reduced the levels of active caspase-3 (n = 4 independent experiments in triplicate, 10/group shown as mean ± SEM; two-tailed t-test: *P < 0.05 versus DMSO). (J–N) Injection of an expression vector encoding zebrafish atg5 into A152T-tau fish embryos resulted in over-expression of Atg5 protein at 2 dpf (J and K) (high and low exposure of the same blot presented; mean ± SD, n = 6 independent clutches; two-tailed t-test, *P < 0.05 versus control). (J and L) The increase in Atg5 protein correlated with increase in LC3II, a well-characterized reporter for autophagosome number, demonstrating that autophagy was upregulated in Atg5-injected fish (mean ± SEM, n = 8 independent clutches; two-tailed t-test, ***P < 0.001 versus control). (M and N) A consistent reduction in the number of offspring with morphological defects was observed in Atg5-injected fish compared to control (uninjected) siblings. The percentage of normal fish changes from 52.43% ± 6.01 to 87.79% ± 4.87 after Atg5 injection and consequently, the proportion of abnormal fish diminishes from 47.57% ± 6.01 to 12.21% ± 4.87 (mean ± SEM of seven independent clutches; two-tailed t-test, ***P < 0.001 versus control). Image collected and cropped by CiteAb from the following open publication (//academic.oup.com/brain/article/140/4/1128/2980948), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

SAN1 functions independently of the FA pathway and does not affect FA pathway activation. a, b CSAs of HeLa WT and SAN1−/− cells treated with scrambled ctrl siRNA or FANCD2 siRNA, in response to Cisplatin and MMC (N = 3). Statistical significance determined by two-way ANOVA. Error bars denote s.e.m. *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. c Immunoblot showing siRNA knockdown of FANCD2 in HeLa WT and SAN1−/− cells. d IF staining of FANCD2 foci in HeLa WT cells and SAN1−/− cells treated with 0.045 μM MMC. e Immunoblot of FANCD2 showing mono-ubiquitylation in HeLa WT and SAN1−/− cells treated with vehicle or 0.045 μM MMC. f, g CSAs of HeLa WT and SAN1−/− cells treated with ctrl or SNM1A siRNA and exposed to Cisplatin or MMC. Statistical significance was determined by two-way ANOVA test. h Immunoblot of SNM1A in HeLa WT and SAN1−/− cells treated with ctrl or SNM1A siRNA Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29968717), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Activation of MAPK7 in chondrocytes is essential for hypoxic adaptation and enhancement of HIF1 alpha signaling under hypoxia. a, b Immunofluorescence staining of (a) MAPK7 (b) P-MAPK7 on representative sections of distal femoral growth plates at P1. Scale bar, 200 μm. RZ, resting zone; PZ, proliferative zone; HZ, hypertrophic zone. c Western blot analysis of MAPK7 and p- MAPK7 in primary chondrocytes cultured under hypoxic conditions for 0, 1, 4, 12, or 24 h. d Immunofluorescence staining of SOX9 on representative sections of distal femoral growth plates at P1. Scale bar, 200 μm. e Western blot analysis of SOX9, COL2A1, MAPK7, HIF1 alpha , and VEGFA in CON and Mapk7 CKO chondrocytes cultured under normoxic or hypoxic conditions for 48 h. f Western blot analysis of SOX9, COL2A1, MAPK7, p-MAPK7, HIF1 alpha , and VEGFA protein levels in XMD8-92- or DMSO-treated primary chondrocytes cultured under normoxic or hypoxic conditions. Primary chondrocytes harvested from wild-type mouse knees were cultured in the presence of 5 μM XMD8-92 or an equal amount of DMSO under normoxia for 3 h, followed by normoxia or hypoxia for 48 h. XMD, XMD8-92. g, h mRNA levels of (g) Sox9 and (h) Col2a1 in CON and Mapk7 CKO chondrocytes cultured under normoxia or hypoxia were measured by real-time quantitative PCR (n = 3). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. i Immunofluorescence staining of HIF1 alpha on representative proximal tibial growth plate sections from P1 mice. Scale bar, 200 μm. j mRNA levels of Hif1a and its known target genes were measured in growth plate cartilage from P1 Mapk7 CKO mice by real-time quantitative PCR. k HIF1 alpha activity in CON and Mapk7 CKO chondrocytes cultured under normoxia or hypoxia, as evaluated by HIF1 alpha -responsive element luciferase reporter (HRE-luc) assay (n = 5). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. l mRNA level of hif1a in CON and Mapk7 CKO chondrocytes cultured under normoxia or hypoxia were measured by real-time quantitative PCR (n = 3). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. m Free ATP levels in CON and Mapk7 CKO chondrocytes cultured under normoxic or hypoxic conditions (n = 4). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. n Primary chondrocytes were transfected with WT-MAPK7 or DN-MAPK7 expression vector in the presence of CA-MEK5 expression vector. Cells were harvested 48 h after transfection and protein levels of HIF1 alpha , MAPK7 and p-MAPK7 were assayed by western blot Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32944217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Caspase-11 is expressed in Casp1Null bone marrow-derived macrophages.Immunoblot analysis of caspase-1, caspase-11 and GAPDH (loading control) in unprimed WT or mutant BMDMs at various times (above lane) after stimulation with IFN-beta (250U/ml), IFN-gamma (100 ng/ml) or LPS (100 ng/ml). Data are representative of two independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28345580), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ZNF217 and ALKBH5 regulate NANOG and KLF4 expression via modulation of m6A levelsA. MCF-7 subclones expressing a non-targeting control shRNA (NTC) or shRNAs targeting HIF-1 alpha and HIF-2 alpha (double knockdown [DKD]), were exposed to 20% or 1% O2 for 48 h. Immunoprecipitation of RNA with m6A antibody and RT-qPCR were performed to determine the percentage of KLF4 mRNA with methylation (m6A+) (mean ± SEM; n = 3). **P < 0.01 vs. NTC at 20% O2; ##P < 0.01 vs. NTC at 1% O2 by two-way ANOVA. B. MCF-7 subclones, which were stably transfected with lentiviral vector expressing NTC or either of two independent shRNAs targeting different nucleotide sequences in ZNF217, were exposed to 20% or 1% O2 for 24 h. Total RNA was extracted and m6A levels were determined as a percentage of all adenosine residues (mean ± SEM; n = 3). *P < 0.05, **P < 0.01 vs. NTC at 20%; ##P < 0.01 vs. NTC at 1% O2 by two-way ANOVA. C and D. MCF-7 subclones were exposed to 20% or 1% O2 for 48 h. The percentage of m6A+ NANOG (C) and KLF4 (D) mRNA was determined (mean ± SEM; n = 3). **P < 0.01 vs. NTC at 20% O2; ##P < 0.01, ###P < 0.001 vs. NTC at 1% O2 by two-way ANOVA. E and F. MCF-7 subclones were exposed to 20% or 1% O2 for 24 h. NANOG (E) and KLF4 (F) mRNA levels were determined. *P < 0.05, **P < 0.01, ***P < 0.001 vs. NTC at 20% O2; ##P < 0.01, ###P < 0.001 vs. NTC at 1% O2 by two-way ANOVA. G. MCF-7 subclones were exposed to 20% or 1% O2 for 48 h and immunoblot assays were performed. H. MCF-7 subclones were exposed to 20% or 1% O2 for 48 h. The percentage of m6A+ KLF4 mRNA was determined. *P < 0.05, **P < 0.01 vs. NTC at 20% O2; ##P < 0.01 vs. NTC at 1% O2 by two-way ANOVA. I. MCF-7 subclones were exposed to 20% or 1% O2 for 24 h and KLF4 mRNA levels were determined. *P < 0.05, ***P < 0.001 vs. NTC at 20% O2; ###P < 0.001 vs. NTC at 1% O2 by two-way ANOVA. J. MCF-7 subclones were exposed to 20% or 1% O2 for 48 h and immunoblot assays were performed. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.11743), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

PML-RARa is a HIF-alpha transcriptional co-activator.A HIF-alpha transactivation assays (A–D) with HRE-luciferase construct. Results are presented as Luciferase/Renilla ratio (mean ± s.e.m. of experiments performed in triplicate).B HEK-293 cells transfected with stable mutants of HIF-1 alpha or HIF-2 alpha and increasing concentrations of PML-RAR alpha .C HEK-293 cells transfected with a stable form of HIF-1 alpha along with PML-RAR alpha , PML or RAR alpha .D Wild-type and Pml−/− MEFs transfected with HIF-1 alpha and PML-RAR alpha . Asterisks indicate fold change induction of HIF-1 alpha -mediated transactivation upon PML-RAR alpha expression.E HEK-293 cells transfected with the indicated fusion genes and treated with CoCl2.F Co-immunoprecipitation of exogenous stable forms of HIF-1 alpha (left panel) and HIF-2 alpha (right panel) and PML-RAR alpha with a PML-directed antibody in HEK-293 cells. Of note, exogenously expressed PML-RAR alpha migrates very closely to endogenous PML.Co-immunoprecipitation of endogenous HIF-1 alpha and PML-RAR alpha with a PML-directed antibody in NB4 cells treated with CoCl2.Data information: All experiments were repeated at least twice.Source data are available for this figure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24711541), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Al, Bv, Dr, Fi, Gp, Pm, Xp, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Al, Bv, Dr, Fi, Gp, Pm, Xp, Ze

Applications:

, , , , , , , , , , ,

Applications: , , , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

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Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB110-53818AF350
Alexa Fluor 405	NB110-53818AF405
Alexa Fluor 488	NB110-53818AF488
Alexa Fluor 532	NB110-53818AF532
Alexa Fluor 594	NB110-53818AF594
Alexa Fluor 647	NB110-53818AF647
Alexa Fluor 700	NB110-53818AF700
Alexa Fluor 750	NB110-53818AF750
Allophycocyanin	NB110-53818APC
Biotin	NB110-53818B
DyLight 350	NB110-53818UV
DyLight 405	NB110-53818V
DyLight 488	NB110-53818G
DyLight 550	NB110-53818R
DyLight 594	NB110-53818DL594
DyLight 650	NB110-53818C
DyLight 680	NB110-53818FR
DyLight 755	NB110-53818IR
FITC	NB110-53818F
HRP	NB110-53818H
PE	NB110-53818PE
PerCP	NB110-53818PCP
mFluor Violet 450 SE	NB110-53818MFV450
mFluor Violet 500 SE	NB110-53818MFV500
mFluor Violet 610 SE	NB110-53818MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-53818SS

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NBP2-12446

NLRP3/NALP3 Antibody - BSA Free

(4 Reviews)

(223 Publications)

0.2 ml

NBP2-12446

C-AR inhibited NLRP3 inflammasome activation in synovial tissue. NLRP3 protein expression in succinate-stimulated synovial fibroblasts. The results were derived from four independent experiments for immunohistochemistry staining and Western blot and expressed as the mean +/- SD. *p 0.05 versus the OA + Allopurinol group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29358971), licensed under a CC-BY licence.

Lycium barbarum polysaccharides lessened the changes in expression of pyroptosis markers (NOD-like receptors protein 3 (NLRP3), caspase-1, and membrane N-terminal cleavage product of GSDMD (GSDMD-N)) in Abeta1-40 oligomers-exposed ARPE-19 cells. (A) Representative immunofluorescence images of NLRP3 (green fluorescence) and DAPI (blue fluorescence) in ARPE-19 cells under different treatments. Abeta1-40 oligomers exposure increased the cellular expressions of NLRP3 (second row). However, the increased expression was subsequently decreased by LBP treatment with both low (3.5 mg/L) and high (14 mg/L) concentration (third row and the fourth row). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32629957), licensed under a CC-BY licence.

Hippocampal AMPK/Sirt1 and NFkappaB/NLRP3/IL-1beta signaling pathways in diabetic rats and the effects of aerobic exercise. Type 2 diabetes significantly decreases the activation of hippocampal AMPK (a) and the level of Sirt1 (c), leading to increased Ac-NFkappaB (d) and NFkappaB (e); diabetic rats contain more NLRP3 inflammasomes (f) and IL-1beta (g). Aerobic exercise intervention significantly increases AMPK activity and Sirt1 concentration; aerobic exercise downregulates the Ac-NFkappaB and NFkappaB, leading to decreased levels of the NLRP3 inflammasome and IL-1beta. **p < 0.01, DM group vs. C group; #p < 0.05, TDM group vs. DM group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30911292), licensed under a CC-BY licence.

Exercise training prevents HFD-induced upregulation of cardiac pyroptosis. Western blotting was performed to determine the components of inflammasome complex and pyroptosis in the left ventricle of mice hearts. (A) HFD-fed obese mice show upregulation of the NLRP3 inflammasome in the left ventricle, which is prevented by exercise training. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31835893), licensed under a CC-BY licence.

NLRP3 deficiency in non-hematopoietic cells exacerbates GVHD and is not rescued by propionate. B6 WT and Gpr43-/- mice received BMT from either syngeneic B6 or allogeneic BALB/c donors. a) Representative immunoblots and densitometric analysis of NLRP3 normalized to the presence of beta-actin in IECs (CD326+) from allogeneic recipients 14 days after BMT (n = 3 each, two-tailed Mann-Whitney U test). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30201970), licensed under a CC-BY licence.

The expression levels of microtubule protein light chain 3 (LC3B), PTEN inducing putative kinase 1 (PINK1), Parkin, mitofusin 1 (Mfn1), toll-like receptor (TLR) 9, cytochrome c oxidase 4 (COX4), myeloid differentiation factor 88 (MyD88), and nuclear factor (NF)-kappa B in lung tissues from animals with spontaneous breathing (CON) or mechanical ventilation at high tidal volume (HTV) with saline, antimycin A (AmA) or cyclosporine A (CsA). (A) Levels of PINK1, Parkin, and Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, and Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I and PINK1 protein. (D) Relative expression of Parkin and Mfn1 protein. (E) Levels of TLR9 and COX4 mRNA. (F) Levels of MyD88 and nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, and NF-kappa B protein by Western blot. (H) Relative expression of TLR9 and COX4 protein. (I) Relative expression of MyD88 and NF-kappa B protein. Fold expression for target genes was normalized to that measured for the beta -actin gene. Both of these experiments were in triplicate. aP < 0.05 vs. CON group;bP < 0.05 vs. HTV group; and cP < 0.05 vs. AmA group. Image collected and cropped by CiteAb from the following open publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Cellular and embryonic localisation of CL-L1.A. Immunostaining of ATDC5 cells with the golgi marker 58K and CL-L1. CL-L1 shows localisation with golgi apparatus (white arrow). B. Laminin and CL-L1 coimmunolocalisation. Laminin shows partial cellular immunolocalisiton with CL-L1 around the golgi area (arrows). Scale bar 50 μm C. Laminin and CL-K1 coimmunolocalisation. CL-K1 staining shows a very strong golgi localisation with partial cytoplasmatic laminin colocalisation. D. CL-L1 immunohistochemistry of a 18.5 days postfertilisation mouse embryo. CL-L1 is expressed in the liver (long arrow) and submucosal patal region (short arrows). E. Immunofluorescence showing co-localisation of CL-L1 and Laminin in E13.5 mouse embryos sections. CL-L1 is expressed in the basal membrane of the ephithelium in the palate shelf of the maxilla (arrows). In contrast Laminin expression is present all around the ephitelium membrane. A faint but clear CL-L1 expression is also observed in the cytoplasm of the epithelium and in the mesenchyme of the palate. PSM; rostral extremity of right palatal shelf of maxilla. Scale bar 100 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28301481), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Role of NF-kappa B in glucose fluctuation-induced inflammasome-related myocardial fibrosis. (A) Immunofluorescence staining of NF-kappa B/p65 nucleation (n = 3 per group). (B,C) The phosphorylation level of NF-kappa B/p65 in rat hearts of the three groups (n = 4 per group). (D) Immunofluorescence staining of intracellular NLRP3–ASC interaction in the GF and GF + TPCA-1 groups. The NRCFs were labeled with anti-NLRP3 (red), anti-ASC (green), and DAPI (blue) (n = 3 per group). (E–G) After application of TPCA-1 (0.5 μM), the protein expressions of cleaved caspase-1 and collagen I were measured by western blot (n = 3 per group). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effects of oltipraz on the expression of CD11b/c, PI3K, p-Akt, and p-IkB alpha in the hippocampus of the CCI-injured mice. The relative protein levels of (A) CD11b/c, (B) PI3K, (D) p-Akt, and (E) p-IKB alpha in the hippocampus of the CCI-injured mice treated with oltipraz (OLT) or vehicle. The sham-operated mice (SHAM) treated with vehicle were used as controls. Representative examples of blots for (C) CD11b/c (160 kDa), PI3K (130 kDa), and GAPDH (37 kDa); and (F) for p-Akt (60 kDa), Akt (60 kDa), p-IKB alpha (40 kDa), and IKB alpha (40 kDa). CD11b/c and PI3K are expressed relative to GAPDH levels whereas phosphorylated proteins are expressed relative to their corresponding total proteins. In all panels, * denotes significant differences vs. sham-operated mice treated with vehicle (p < 0.05; one-way ANOVA followed by the SNK test). Results are presented as the mean ± SEM; n = 5 samples per experimental group. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31234342), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRRK2 regulation on alpha -synuclein levels. a Western blot analysis of basal alpha -synuclein and b p62 levels in neurons during mid and late differentiations. Blots show the alpha -synuclein soluble monomer of ~15 kDa. Bars represent the mean ± SEM of three to six values, including two different cell lines per group. beta III-tubulin was used as loading control (two-way ANOVA, ** P < 0.01, LRRK2G2019S v. control WT, late stage). cLRRK2 RNA levels 5 days after shRNA lentiviral transduction. The empty vector was used as the mock control. Lines represent the mean ± SEM of three to four independent silencing experiments. A representative immunoblot analysis of LRRK2 protein levels 5 days after transduction is also shown. beta III-tubulin was the loading control. d Immunoblots and corresponding quantification of alpha -synuclein 5 days after shLRRK2 transduction. Bars represent the mean ± SEM of at least three independent silencing experiments. LRRK2 silencing had a significant effect on alpha -synuclein protein levels (two-way ANOVA, *** P = 0.0002). Bonferroni post hoc test showed that this effect was limited to LRRK2 mutated mature neurons (**P < 0.05 for both LRRK2G2019S and LRRK2R1441G). e qRT-PCR analysis of SNCA after LRRK2 silencing. f Immunoblots and corresponding quantification of p62 5 days after shLRRK2 transduction. Bars represent the mean ± SEM of at least three independent silencing experiments. See Additional file 3 for uncropped blots Image collected and cropped by CiteAb from the following open publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-016-0761-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ER stress is induced by acidosis activated OGR1-mediated signalling. Caco-2 cells were subjected to different pH medium, following 4–6 h incubation in pH 7.6 serum free medium. (A) Vector control Caco-2 (VC) and OGR1 overexpressing Caco-2 cells where treated with tunicamycin at the indicated concentrations for 24 h. Total protein was isolated and Western blotting was performed. The results are representative of two independent experiments. (B) After 24 h pH shift, total protein was isolated and Western blotting was performed. The results are representative of three independent experiments. (C) Densitometry after normalization of BiP to beta -actin and (D) p-IRE1 alpha to total IRE1 alpha . Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (*p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001). (E) After 24 h pH shift, total RNA was isolated and mRNA expression was investigated by qPCR. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (*p < 0.05; **p < 0.01). (F) A specific small molecule OGR1 inhibitor (10 µM) was tested and the cells were subjected to low pH for 24 h, following 4–6 h incubation in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated and Western blot performed. Results are representative of two independent experiments. (G) Cells were treated as described in (F), then total RNA was extracted and analysed for expression of XBP1 (XBP1u) and spliced XBP1 (XBP1s) by conventional PCR. Results are representative of three independent experiments. (H) Quantification of the ratio of XBP1s/XBP1u was performed using ImageJ. Results are representative of two independent experiments. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (*p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001). For all the panels, the experiments were repeated two to three times. pH conditions: High pH 7.5–7.8; Normal pH 7.2–7.4; Low pH 6.6–6.8. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31996710), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Flow cytometry gating strategy for quantification of platelet-derived microparticles in equine platelet samples.A: Platelet events in citrate-anticoagulated platelet-rich plasma were identified and gated as CD41-positive cells (R1 region) in a CD41 fluorescence versus forward scatter (FSC) dotplot. The R1 region or gate was established on an isotype control for the CD41 antibody. Representative image from platelets exposed to the RacL11 strain of EHV-1 at 1 plaque forming unit (PFU)/cell. B: Platelet-derived microparticles (PDMPs) were defined as small events (<101 log FSC units) positive for Annexin V and CD41. The PDMP percentage was obtained from the lower right quadrant of an Annexin V fluorescence versus FSC dotplot of the R1 gate (CD41-positive events), with the quadrants being defined on a negative sample in which 1 mM EDTA was added to the buffer with Annexin V. The PDMP percentage was 0.1% in this representative image of platelets exposed to rabbit kidney 13 (RK) cell lysate at an equivalent volume to 1 PFU/cell (mock-infected negative control). The events in the upper left and right quadrants are platelets that are negative (94.0%) and positive for Annexin V (0.9%), respectively. C: Representative image of PDMP quantification in platelets exposed to RacL11 at 1 PFU/cell. In this sample, there are 12.1% PDMP (lower right quadrant) and 22.1% of platelets are weakly positive for Annexin V (upper right quadrant). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25905776), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, RM

Species Glossary

Reactivity: Hu, Mu, Rt, RM

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-6668A

Alt Catalog# IMG-6668A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-12446AF350
Alexa Fluor 405	NBP2-12446AF405
Alexa Fluor 488	NBP2-12446AF488
Alexa Fluor 532	NBP2-12446AF532
Alexa Fluor 594	NBP2-12446AF594
Alexa Fluor 647	NBP2-12446AF647
Alexa Fluor 700	NBP2-12446AF700
Alexa Fluor 750	NBP2-12446AF750
Allophycocyanin	NBP2-12446APC
Biotin	NBP2-12446B
DyLight 350	NBP2-12446UV
DyLight 405	NBP2-12446V
DyLight 488	NBP2-12446G
DyLight 550	NBP2-12446R
DyLight 594	NBP2-12446DL594
DyLight 650	NBP2-12446C
DyLight 680	NBP2-12446FR
DyLight 755	NBP2-12446IR
FITC	NBP2-12446F
HRP	NBP2-12446H
Janelia Fluor 549	NBP2-12446JF549
Janelia Fluor 646	NBP2-12446JF646
PE	NBP2-12446PE
PerCP	NBP2-12446PCP

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-12446SS

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NB100-56708

Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free

(2 Reviews)

(191 Publications)

0.1 mg

NB100-56708

Image of Caspase-3 Antibody (31A1067) - (Pro and Active). Whole cell protein from Jurkat cells treated with and without 2 uM staurosporine as indicated was separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 5 ug/ml anti-Caspase 3 in 1% milk, and detected with an anti-mouse HRP secondary antibody using a Femto sensitivity chemiluminescence reagent. Note the detection of both pro-caspase 3 at 35 kDa and the cleaved active caspase 3 at 15-17 kDa.

<b>Biological Strategies Validation. </b>Tissue section of human spleen using 1:200 dilution of Caspase-3 antibody (clone 31A1067). The staining was developed with HRP labeled anti-mouse IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This Caspase 3 antibody generated primarily a specific cytoplasmic staining in a subset of spleenocytes with some nuclear signal in a few cells.

Simple Western lane view shows a specific band for Caspase-3 Antibody (31A1067) - (Pro and Active) in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230kDa separation system.

Caspase-3 was detected in immersion fixed paraffin-embedded sections of human bladder tissue using 1:50 dilution of mouse aCaspase-3 Antibody (31A1067) - (Pro and Active) (NB100-56708), for 1 hour at room temperature followed by anti-mouse IgG VisUCyte HRP polymer(VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue).

Paclitaxel in combination with MWE retarded tumor growth in a human bladder carcinoma TSGH 8301 xenograft model. The levels of total (t-PTEN) and phospho-PTEN (p-PTEN) and Caspase 3 in the tumor specimens were determined by Western blotting and then quantified using beta-actin as the protein loading control; the results are expressed as a percentage of the control. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep20417), licensed under a CC-BY license.

An intracellular stain was performed on NIH3T3 cells with Caspase-3 Antibody (31A1067) - (Pro and Active) Antibody NB100-56708AF700 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 700.

<b>Biological Strategies Validation. </b>Lysates of Jurkat human acute T cell leukemia cell line untreated (-) or treated (+) with VP-16. PVDF membrane was probed with 0.1 ug/mL of mouse monoclonal Caspase-3 Antibody (31A1067) - (Pro and Active) (NB100-56708, Novus Biologicals) followed by 1:2000 dilution donkey anti-mouse IgG.

An intracellular stain was performed on HeLa cells with Caspase-3 Antibody (31A1067) - (Pro and Active) NB100-56708 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems).

$NFATc1 regulates DcR3 expression at a transcriptional level. (C) Immunoblot analysis of cytoplasmic and nuclear fractions of ACHN and 769-P cells after treatment with LY294002 (50 uM), Everolimus (1 uM), or Cyclosporine A (25 uM). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24107265), licensed under a CC-BY licence.$

Lipofection of top broccoletti-miR candidates does not influence basal and induced apoptosis. (B) Lipofected BxPc-3 and Bx-Gem cells were stained with an antibody specific for the proliferation marker Ki-67 (green) or the apoptosis marker cleaved fragment of caspase-3 (red), which indicates apoptosis. Representative images at x100 magnification are shown. The percentage of Ki-67- or caspase-3-positive cells was counted in 18 visual fields, and the means +/- SD are shown in the diagram below. (C) BxPc-3 and Bx-Gem were lipofected as described above, and at 24 h later, the cells were treated with gemcitabine (10 nM) or were left untreated. Ninety-six hours after gemcitabine treatment, viability was determined by MTT assay. The data are presented as the means +/- SD (**P < 0.01). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32292571), licensed under a CC-BY licence.

Western Blot: Mouse Monoclonal Caspase-3 Antibody (31A1067) - (Pro and Active) [IMGENEX: IMG-144A] [NB100-56708] - Whole cell lysates from MDA-MB-231, MCF-7, SUM149 and SUM159 cells were loaded with 50 ug/lane. 10% SDS-PAGE. Caspase-3 Antibody (NB100-56708) was used for primary antibody: 1:2000, 4℃, overnight. Image from a verified customer review.

APE1 acetylation enhances its stability on chromatin and its interaction with downstream BER proteins. (A) Colocalization of ligase III and AcAPE1 in A549 cells. Cells were immunostained with anti-ligase III and anti-AcAPE1 Abs. (B) WT or K5R mutant APE1-overexpressing HEK293T cells were treated with TSA-nicotinamide (NAM) for 6 h or not treated, and the nuclear extract was immunoprecipitated using anti-FLAG Ab and immunoblotted with anti-XRCC1 and anti-FLAG Abs. (C) A549 cells were fixed with paraformaldehyde before (top) or after treatment with Triton X-100 (0.5%) (middle) or Triton X-100 plus salt (100 mM KCl) (bottom) and immunostained with anti-APE1 or anti-AcAPE1 Abs and counterstained with DAPI. (D) Acetylation of APE1 induces a conformational change in APE1. The distinct intrinsic fluorescence emission spectra of APE1 and AcAPE1 at 280 nm are shown. A.U., absorbance units. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reduced expression levels of IFI16 protein in human normal diploid fibroblasts after treatment with histone deacetylase inhibitor are associated with increased expression of hTERT and increased telomerase activity.(A) Total RNA isolated from untreated (control, lane 1) or CGK1026 (10 µM for 24 h, lane 2) treated young WI-38 fibroblasts was subjected cDNA synthesis followed by semi-quantitative PCR using a pair of primer specific to the IFI16, hTERT, or actin. As a positive control, we used RNA from human HT1080, a human fibrosarcoma cell line. (B) Total RNA isolated from untreated (control) or CGK1026 (10 µM for 24 h; treated) treated young WI-38 fibroblasts was subjected cDNA synthesis, followed by quantitative real-time PCR using the TaqMan assay for the hTERT gene. Results are mean values of triplicate experiments and error bars represent standard deviation (**p<0.005). (C and D) Total protein extracts prepared from untreated (lane 1) or CGK1026 (10 µM for 24 h; treated) treated young WI-38 fibroblasts were subjected to immunoblotting using antibodies specific to the indicated proteins. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0008569), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

HIF-1 alpha overexpression rescues oxygen-induced radioresistance in RAH-treated cells, but not GCH-treated cells.Results are shown for the anchorage-independent colony forming assays for U87 cells transfected with either an empty vector or HIF-1 alpha expression vector and then exposed to GCH or RAH protocols without (–) or with (+) reoxygenation. Continuously normoxic cells (NOx) were irradiated as a positive control. To allow for ease of comparisons among conditions, raw values are presented as a percentage of that cell type’s negative (non-irradiated) control and the means and SEMs are plotted. Each result represents at least three independent samples, plated in triplicate. Holm-Sidak comparisons for multiple groups were used for statistical comparisons of raw values (*p<0.05, **p<0.01). Western blotting analysis of nuclear HIF-1 alpha at the time of irradiation is shown for each cell type below clonogenic results. Corresponding Western blots of lamin A/C are shown as a loading control and blots for hemagglutinin (HA) are shown below HIF-1 alpha overexpression vector results to demonstrate transfection efficacy. All lanes shown that are non-adjacent to the negative control (NOx) are denoted with a separating black line. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25350400), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Differential roles of caspase-1 and caspase-11 in response to infection with Aspergillus fumigatus.(A) Immunoblot analysis of pro-caspase-1 (Pro-Casp-1) and the caspase-1 subunit p20 (Casp-1 p20) and GAPDH (loading control) in unprimed WT or mutant bone marrow-derived dendritic cells left untreated (medium alone [Med]) or assessed 20 h after infection with A. fumigatus (MOI, 10). (B) Release of IL-1 beta and IL-18 after treatment as in (A). (C) Survival of 8-week-old WT and mutant mice infected with 5 × 105 A. fumigatus conidia after immunosuppression with cyclophosphamide and cortisone acetate. *P < 0.05, ****P < 0.0001 (log-rank test). Data are representative of two (C) or three independent experiments (A and B; mean and s.e.m. are representative of values from three independent experiments in B). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28345580), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ch, ChHa, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ch, ChHa, Ma

Applications:

, , , , , , , , , , ,

Applications: , , , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-144A

Alt Catalog# IMG-144A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-56708AF350
Alexa Fluor 405	NB100-56708AF405
Alexa Fluor 488	NB100-56708AF488
Alexa Fluor 532	NB100-56708AF532
Alexa Fluor 594	NB100-56708AF594
Alexa Fluor 647	NB100-56708AF647
Alexa Fluor 700	NB100-56708AF700
Alexa Fluor 750	NB100-56708AF750
Allophycocyanin	NB100-56708APC
Biotin	NB100-56708B
DyLight 350	NB100-56708UV
DyLight 405	NB100-56708V
DyLight 488	NB100-56708G
DyLight 550	NB100-56708R
DyLight 594	NB100-56708DL594
DyLight 650	NB100-56708C
DyLight 680	NB100-56708FR
DyLight 755	NB100-56708IR
FITC	NB100-56708F
HRP	NB100-56708H
Janelia Fluor 549	NB100-56708JF549
Janelia Fluor 646	NB100-56708JF646
PE	NB100-56708PE
PerCP	NB100-56708PCP
mFluor Violet 450 SE	NB100-56708MFV450
mFluor Violet 500 SE	NB100-56708MFV500
mFluor Violet 610 SE	NB100-56708MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56708SS
Azide and BSA Free	NBP2-33244

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NB100-132

HIF-2 alpha/EPAS1 Antibody (ep190b)

(9 Reviews)

(184 Publications)

0.1 ml

NB100-132

Immunohistochemistry-Paraffin: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Analysis of HIF-2 in human cardiac myocytes using HIF-2 alpha/EPAS1 Antibody (ep190b).

Flow Cytometry: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - HIF-2 alpha antibody was tested at 1:400 in HepG2 cells using an Alexa Fluor 488 secondary (shown in purple). M1 is defined by unstained cells.

Western Blot: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Mouse aortic endothelial cells treated (1%) or not treated (20.9%) in hypoxia for 3 hrs. Cells where also transfected with a specific siRNA against (siHIF-2) or a control siRNA (-). Western blot image submitted by a verified customer review.

Immunohistochemistry-Paraffin: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Renal tubule specific models of Vhl deletion. Histological images of representative renal sections from 12 month old control, Pax8-CreERT2/Vhldelta/delta and Slc22a6-CreERT2/Vhldelta/delta mice (stains and antibodies as indicated, arrowheads indicate abnormal vascularization). Scale bars, 100 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0148055), licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Western Blot: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Analysis of HepG2 without Cobalt (II) Chloride (1), HepG2 with Cobalt (II) Chloride (2), HepG2 normoxic (3), HepG2 hypoxic (4), HepG2 without Cobalt (II) Chloride (5), HepG2 with Cobalt (II) Chloride (6), HepG2 normoxic (7), and HepG2 hypoxic (8) using this antibody (NB100-132) at 1 - 2 ug/mL.

<b>Biological Strategies Validation. </b>Western Blot: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - [HRP] [NB100-132H] - Analysis of HIF-2 alpha stabilization over time in HOS cells following exposure to hypoxia. Image using the HRP form of this antibody (NB100-132H). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23785417/) licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Western Blot: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Western blot analysis and quantification of HIF-2 alpha expression in the cortex 4.5 hours after lipopolysaccharide (LPS) administration for all LPS groups and the control group (SHAM, white bar). With the exception of the vagotomy group (VGX LPS, gray bar), no significant differences to the SHAM group were found in the LPS-treated and sham-operated (SHAM+LPS, light gray bar) or vagus nerve-stimulated groups (VGX LPS+STIM, black bar). The significant increase in the VGX LPS (gray bar) group is an indicator of a hypoxic condition; * P<0.05 compared to SHAM; n=6 rats each. Data are given as the mean+/-SEM. Image collected and cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-183), licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Western Blot: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - 4-OOHCPA exposure induced HIF-2 alpha/EPAS1. A: Western blot analysis of HIF-2 alpha/EPAS1 protein (118KD) and actin (43KD) in limbs at 10 min, 1, 3, 6, and 24 h after treatment with 4-OOHCPA at 0.3 ug/mL (L) 1.0 ug/mL (M) or 3.0 ug/mL (H). P represents the positive control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0051937), licensed under a CC-BY license.

Immunohistochemistry: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Analysis of HIF-2 alpha in human endometrium using. Donkey anti-mouse Alexa Fluor 488 secondary antibody was used. IHC image submitted by a verified customer review.

<b>Biological Strategies Validation and Genetic Strategies Validation.</b>Knockdown Validated: HIF-2 alpha/EPAS1 Antibody (ep190b) [NB100-132] - Functional role of HIF2A in the transcriptional regulation of amphiregulin (AREG) in human cardiac myocytes. Immunoblot for HIF1A or HIF2A from shRNA-transfected normoxic or hypoxic HCM. Beta-Actin (ACTb) served as a loading control. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29483579/) licensed under a CC-BY license.

In vitro effects of diclofenac on proliferation and MYC expression in the human melanoma cell line MelIm. (E-G) MYC, STAT3, HIF1a and HIF2a protein expression were determined in cell lysates of MelIm incubated for 2 or 24 h with or without diclofenac (E,F) or ASA (G). The effect of diclofenac on MYC promoter activity was determined by transient transfection of a 2632-bp MYC promoter fragment (H). MelIm were transfected in 6-well-plates and diclofenac was added after 5 h. Luciferase activity was determined 24 h after transfection. Results represent the mean +/- standard deviation of 3 independent experiments. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0066987), licensed under a CC-BY licence.

BAY 87-2243 inhibits hypoxia-inducible factor (HIF-1alpha) and HIF-2alpha protein accumulation in hypoxic H460 cells H460 under hypoxia but has no effect on HIF-1alpha protein levels induced by hypoxia mimetics and has no effect on prolyl hydroxylase 2 (PHD2) activity. (A, B) H460 cells were cultured for 16 h under normoxia or hypoxia (1% pO2) in the absence or presence of various concentrations of BAY 87-2243. HIF-1alpha (A) and HIF-2alpha (B) protein levels were assessed by Western Blot in whole cell extracts. beta-actin was used as a loading control. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24403227), licensed under a CC-BY licence.

HIF2alpha inhibitor 76 suppressed CoCl2-induced immature phenotypic characteristics of BCSCs. (A) The inhibitory effect of small molecule HIF2alpha inhibitor 76 for 24h (10 uM for 4T1 cells; 25 uM for Hs578T cells) on CoCl2-induced expression of HIF2alpha was assessed in both 4T1 and Hs578T cells by western blot analysis. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.9846), licensed under a CC-BY licence.

Hypoxic repression of ER-alpha is dependent on HIF-1alpha. a Representative western blots of HIF-1alpha, HIF-2alpha and beta-actin protein in ten ER-positive cell lines grown at normoxia or hypoxia (1% O2, 24 h). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28320353), licensed under a CC-BY licence.

Western blot analysis and quantification of HIF-2alpha expression in the cortex 4.5 hours after lipopolysaccharide (LPS) administration for all LPS groups and the control group (SHAM, white bar). With the exception of the vagotomy group (VGX LPS, gray bar), no significant differences to the SHAM group were found in the LPS-treated and sham-operated (SHAM + LPS, light gray bar) or vagus nerve-stimulated groups (VGX LPS + STIM, black bar). The significant increase in the VGX LPS (gray bar) group is an indicator of a hypoxic condition; * P < 0.05 compared to SHAM; n = 6 rats each. Data are given as the mean +/- SEM. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22830560), licensed under a CC-BY licence.

Cytosol-restricted Acss2 is enzymatically active.(A) Acetylation of ectopic HA-tagged HIF-2alpha detected by immunoblotting (IB) with anti-HA or anti- acetylated lysine antibodies following immunoprecipitation (IP) with anti-HA antibody in stably transformed HT1080 cells with knockdown of endogenous Acss2 and rescue with ectopic wild-type (WT) or cytosol-restricted mutant (CYT) Acss2 without or with an SV40 nuclear localization signal fused to the amino terminus. Studies were performed under hypoxia, low glucose, or acetate exposure for the indicated periods. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0190241), licensed under a CC-BY licence.

$Localisation of CDS1 immunoreactivity and CDS activity to mitochondria.[A, B] Differentiated H9c2 cells fractionated and analysed for [A] CDS1 immunoreactivity by Western blot; [B] CDS activity. [C-E] Rat heart fractionated and analysed for [C] CDS1 immunoreactivity and markers, [D] CDS1 immunoreactivity (entire Western blot shown) and [E] CDS activity. [F–H] Rat heart fractionated in the presence of the protease, subtilisin and analysed for [F] CDS1 immunoreactivity by western blot, [G] CDS activity and [H] PI synthase (PIS) activity. CDS and PIS activity was monitored in triplicate and error bars denote ± S.E.M. COXIV, GRP75 and cyto c are markers for mitochondria, PITPNC1 and PITP alpha are cytosolic markers and calnexin is a marker for the ER. WCL, whole cell lysate; Micro, microsomes; C.Mito, crude mitochondria; Cyto, cytosol; P.Mito, pure mitochondria, MAMs, mitochondrial associated membranes; PIS, PI synthase; CDS, CDP-diacylglycerol synthase. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29253589), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Effect of overexpression or knockdown of PAL31 in C6 on H2O2-induced toxicity. (A) Representative micrographs showing C6 overexpressing GFP or GFP-tagged PAL31 after being treated with H2O2 (0 ~ 1 mM) for 4 hours. (B) MTT assay in GFP- or GFP-PAL31-overexpressed C6 after H2O2 treatment showing significant difference (cytoprotective effect of PAL31) at 0.5 mM and 1 mM H2O2 treatment between C6/GFP and C6/PAL31 groups. The data in each dosage were analyzed by two-way ANOVA and Bonferroni post hoc test. *P < 0.05, GFP (+H2O2) compared to PAL31 (+H2O2), n = 4, at 0.5 mM and 1 mM. (C) Western blot analysis of pal31 siRNA-treated C6 showing knockdown of PAL31 expression by PAL31 silencer using 41.5 (lane1), 83 (lane2), and 166 (lane 3) picomole of pal31 siRNA or 332 picomole negative control. Actin works as a loading control. (D) MTT assay in Negative- or PAL31 silencer transfected C6 after H2O2 treatment showing significant difference at 1 mM H2O2 treatment between C6/Negative and C6/PAL31 siRNA groups. *P < 0.05, Negative (+H2O2) compared to PAL31 siRNA (+H2O2), n = 4. Magnification 100X (A). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25034417), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Expression of PRDX2 or PRDX4 does not affect HIF-1 alpha or HIF-2 alpha protein levelsA. and B. HeLa cells were transfected with EV or vector encoding PRDX2-V5 (A, P2) or PRDX4-V5 (B, P4), and exposed to 20% or 1% O2 for 24 h. WCL was subject to immunoblot assays with antibody against HIF-1 alpha , HIF-2 alpha , V5, or acin. C. HeLa-shSC (sc) and HeLa-shPRDX(2+4) (2+4) cells were exposed to 20% or 1% O2 for 24 h in the presence of doxycycline. WCL was subject to immunoblot assays with antibodies against HIF-1 alpha , HIF-2 alpha , PRDX2, PRDX4, and actin. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.7142), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GAS6 triggers p-Axl, p-DAPK and CIP2A to form a protein complex in RSC96 cells(A-B) Co-immunoprecipitation between p-Axl, p-DAPK and CIP2A with GAS6 stimulation for 30 min in RSC96 cells. Total lysate indicates 1/10 input in each experiment. The relative quantification of protein expression was normalized with respect to beta -actin expression. (C) Immunofluorescence image demonstrating co-localized CIP2A and p-Axl and co-localized p-Axl and p-DAPK (D) after GAS6 stimulation for 30 min in RSC96 cells. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.23978), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

FKBP51 increases expression of melanoma CSC markers. (a) FKBP51 silencing decreases ABCB5 levels. (Left) Normalized expression rates (arbitrary units (AU)) (mean±S.D.) of FKBP51 (black) and ABCB5 mRNA (grey) (n=3). FKBP51-treated sample expression=1. (Right) Western blot assay of ABCB5 and FKBP51 levels. (b) FKBP51 overexpression enhances ABCB5 levels. (Left) Normalized expression of FKBP51 mRNA (black) and ABCB5 mRNA (grey) measured in WT, EV-, or FKBP51-stably transfected melanoma cells. WT sample expression=1; n=3. (Left) Western blot assay of ABCB5 and FKBP51 levels in the same cells. Anti-Flag-labelled exogenous FKBP51. (c) ABCG2+ melanoma cells increase in FKBP51-overexpressing cells. (Upper) Normalized expression of FKBP51 mRNA (black) and ABCG2 mRNA (grey) measured in WT, EV-, or FKBP51-stably transfected melanoma cells. WT sample expression=1; n=5. (Lower) Flow cytometric histograms of ABCG2 expression (green population); mean±S.D. of counts are shown. (d) Enhanced FKBP51 mRNA levels in sorted ABCG2+ melanoma cells (SAN, upper; A375, lower). Whole cell expression=1; (n=3). (e) Enhanced EMT gene transcripts in sorted ABCG2+ melanoma cells. ABCG2− sample expression=1; n=3. (f) Expression of ABCG2 transcript in 9 deparaffinized tumours, 4 primary melanoma (M) samples, and 5 metastases (MM). A naevus sample was arbitrarily chosen with expression=1 Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/cddis2013109), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Spy1 stable protein accelerates tumorigenesis in vivo.(A) Percentage of mice presenting with palpable tumors from 0-19 days post-transplant. Each data point represents 4 mice per indicated construct. The entire experiment was repeated three times using three independently derived overexpressing cell lines for each construct. Mann-Whitney Test was performed (p < 0.05). (A; lower blot) Western blots were conducted to measure the stability of Myc-Spy1-WT (left) and Myc-Spy1-TST (right) from representative time points. Empty vector control (Cntl) cell expression levels of Spy1 are seen in lane 1 of each blot. (B) Total tumor volume was calculated for both Spy1-HC11 (Spy1-WT) and Spy1-TST-HC11 (Spy1-TST) transplanted glands. Results were taken from 45 transplants using cells from 3 separate transfections. Error bars reflect SE between transplants from different transfections. Left hand panel reflects overall volume, right hand panel reflects volumes of tissues taken over a month post-transplant. Image collected and cropped by CiteAb from the following open publication (//bmccancer.biomedcentral.com/articles/10.1186/1471-2407-12-45), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Livin staining in normal adrenal glandLivin staining in normal adrenal gland (A). It is possible to recognize the three different zone of the adrenal gland: the zona glomerulosa (ZG), the zona fasciculata (ZF) and the zona reticularis (ZR). The Figures (B) and (C) are 20× enlarged and detailed images of the 10× ZG, ZF and ZR, respectively. Scale bar: 100 μm. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14067), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Curcumin Analogs Induce Apoptosis in Cancerous Cells by Several Pathways. (a) E6-1 (Jurkat), dominant negative FADD (dnFADD) Jurkat, and overexpressing BCL-2 Jurkat were treated for 48 hours then stained for Annexin V and PI (b) E6-1 cells were plated and treated with or without the broad spectrum caspase inhibitor ZVAD(oMe)-FMK for 48 hours. Cells were stained for Annexin V and PI. Results were obtained using image-based cytometry with the Y-axis representative of percent of cells positive for Annexin V (green), PI (red), Annexin V and PI (yellow), or negative for both Annexin V and PI (blue). Values are expressed as a mean ± SD from three independent experiments. (c) E6-1 cells were treated for 24 hours with or without the broad spectrum caspase inhibitor ZVAD(oMe)-FMK and the studied compounds, lysed and subjected to Western blot analysis. (d) NHF and NCM460 cells were treated for 48 hours and 72 hours respectively, lysed and subjected to Western blot analysis. Bands were visualized with a chemiluminescence reagent. Images are representative of three independent experiments. Statistical calculations were performed using Two-Way ANOVA multiple comparison. *p < 0.05 vs % viable of Control (DMSO); #p < 0.05 vs % viable cells for groups without Z-VAD(oMe)FMK. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28439094), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effect of TSA treatment on the subcellular localization of Crm1.Control ES or Nup98-HoxA9 expressing ES cells were cultured in the presence or absence of 50 nM TSA for 24 hr. Then, the cells were fixed and stained with antibodies against FLAG (M2) and Crm1. Merged images of FLAG (green) and Crm1 (red) are shown. Nuclei were stained with DAPI. Bar, 10 μm. DAPI, 4',6-diamidino-2-phenylindole; ES, embryonic stem; TSA, trichostatin A.DOI://dx.doi.org/10.7554/eLife.09540.020 Image collected and cropped by CiteAb from the following open publication (//elifesciences.org/articles/09540), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Bv, Ha

Species Glossary

Reactivity: Hu, Mu, Rt, Bv, Ha

Applications:

, , , , , , , , , , ,

Applications: , , , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-132AF350
Alexa Fluor 405	NB100-132AF405
Alexa Fluor 488	NB100-132AF488
Alexa Fluor 532	NB100-132AF532
Alexa Fluor 594	NB100-132AF594
Alexa Fluor 647	NB100-132AF647
Alexa Fluor 700	NB100-132AF700
Alexa Fluor 750	NB100-132AF750
Allophycocyanin	NB100-132APC
Biotin	NB100-132B
DyLight 350	NB100-132UV
DyLight 405	NB100-132V
DyLight 488	NB100-132G
DyLight 550	NB100-132R
DyLight 594	NB100-132DL594
DyLight 650	NB100-132C
DyLight 680	NB100-132FR
DyLight 755	NB100-132IR
FITC	NB100-132F
HRP	NB100-132H
PE	NB100-132PE
PerCP	NB100-132PCP
mFluor Violet 450 SE	NB100-132MFV450
mFluor Violet 500 SE	NB100-132MFV500
mFluor Violet 610 SE	NB100-132MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Azide and BSA Free	NBP2-80766

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NB500-249

Beclin 1 Antibody - BSA Free

(9 Reviews)

(154 Publications)

0.1 ml

NB500-249

Immunohistochemistry: Beclin 1 Antibody - BSA Free [NB500-249] - Detection of Beclin 1 (red) in Pheochromocytes of the Adrenal Medulla 40x.

Flow Cytometry: Beclin 1 Antibody - BSA Free [NB500-249] - An intracellular stain was performed on U-87MG cells with Beclin 1 Antibody NB500-249 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).

Western Blot: Beclin 1 Antibody - BSA Free [NB500-249] - Representative Western blot images and quantitative analyses of Beclin 1 from the left hemisphere of rat brains at different time points after SAH. Sample size is 36, n = 6 per group. Data were presented as mean +/- SD. F = 12.37 for Beclin 1. *P 25 cells each. (E) GamGFP forms IR-induced foci in Ku80-defective MEFs. (F) Zoomed image from E. (G) IR-induced foci containing Gam only, 53BP1 only or both Gam and 53BP1 (>2600 total foci counted in three independent experiments). Error bars, SEM. Scale bars = 5 μm.DOI:
//dx.doi.org/10.7554/eLife.01222.012GamGFP marks DSBs in mammalian cells.(A) Live analysis of GamGFP localization to laser-induced DNA damage. Hela cells producing GamGFP were laser damaged along the cell track indicated by the red line at 0 min (m) and images were taken at the indicated times as shown. (B) GamGFP co-localizes with gamma H2AX in fixed Hela cells.DOI:
//dx.doi.org/10.7554/eLife.01222.013Ku inhibits GamGFP recruitment at DSBs independently of non-homologous end joining.Cells lacking either Ku80 or LigIV are defective in non-homologous end joining (NHEJ), yet the presence of Ku still inhibits recruitment of GamGFP to laser-induced DSBs even in NHEJ-defective cells, and thus independently of the cell's ability to complete NHEJ. Whereas it could have been possible that reduced GamGFP recruitment in the presence of Ku was caused by reduced persistence of DSBs due to their repair by NHEJ, our data show instead that Ku inhibits recruitment independently of successful NHEJ and imply that Ku binding to DSEs itself is inhibitory.DOI:
//dx.doi.org/10.7554/eLife.01222.014 Image collected and cropped by CiteAb from the following open publication (//elifesciences.org/articles/01222), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB500-249AF350
Alexa Fluor 405	NB500-249AF405
Alexa Fluor 488	NB500-249AF488
Alexa Fluor 532	NB500-249AF532
Alexa Fluor 594	NB500-249AF594
Alexa Fluor 647	NB500-249AF647
Alexa Fluor 700	NB500-249AF700
Alexa Fluor 750	NB500-249AF750
Allophycocyanin	NB500-249APC
Biotin	NB500-249B
DyLight 350	NB500-249UV
DyLight 405	NB500-249V
DyLight 488	NB500-249G
DyLight 550	NB500-249R
DyLight 594	NB500-249DL594
DyLight 650	NB500-249C
DyLight 680	NB500-249FR
DyLight 755	NB500-249IR
FITC	NB500-249F
HRP	NB500-249H
Janelia Fluor 549	NB500-249JF549
Janelia Fluor 646	NB500-249JF646
PE	NB500-249PE
PerCP	NB500-249PCP
mFluor Violet 450 SE	NB500-249MFV450
mFluor Violet 500 SE	NB500-249MFV500
mFluor Violet 610 SE	NB500-249MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB500-249SS

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NB100-309

ATM Antibody (2C1)

(3 Reviews)

(130 Publications)

100 ul

NB100-309

Western Blot: ATM Antibody (2C1) [NB100-309] - Detection of human ATM protein using ATM antibody (2C1) [NB100-309] by western blot or immunoprecipitation. Theoretical molecular weight 351 kDa.

Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human breast carcinoma. ATM stained by ATM antibody [2C1] diluted at 1:100.Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.

Western Blot: ATM Antibody (2C1) [NB100-309] - Analysis of ATM in U2OS sarcoma cells using ATM antibody (2C1) [NB100-309]. Theoretical molecular weight 351 kDa. Western blot image submitted by a verifeid customer review.

Western Blot: ATM Antibody (2C1) [NB100-309] - Whole cell extract (30 ug) was separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (2C1) [NB100-309] diluted at 1:1000. Theoretical molecular weight 351 kDa.

Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human Kidney (formalin-fixed, paraffin-embedded) stained with ATM antibody (2C1) [NB100-309] at 5 ug/ml followed by biotinylated anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen.

Knockdown Validated: ATM Antibody (2C1) [NB100-309] - Non-transfected (-) and transfected (+) HeLa whole cell extracts (60 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (2C1) [NB100-309] diluted at 1:500.

<b>Genetic Strategies Validation. </b>Knockdown Validated: ATM Antibody (2C1) [NB100-309] - Methylated EDSBs may be repaired by an ATM-dependent pathway. Immunoblots of ATM and DNA-PKcs in ATM shRNA-transfected HeLa cells, using ATM antibody (2C1) [NB100-309]. GAPDH is included as a loading control. Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-9-70), licensed under a CC-BY license.

Immunoprecipitation: ATM Antibody (2C1) [NB100-309] - MDA-MB-231 whole cell lysates were immunoprecipitated with 2 ug ATM Antibody (NB100-309), followed by Western blot (primary antibody: NB100-309 at 1:1000, 4C overnight. Western blot image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - MCELNs decreased the DNA damage of H9C2 cells after radiation. Western blot images of p-ATM (NB100-306) and ATM (NB100-309) in H9C2 cells after 48 h of culture with indicated treatment. IR (-/+): 0/16 Gy X-ray; MCELNs (-/+): 0/10 ug/mL. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35509278/) licensed under a CC-BY license.

Western blot analysis of the extent of knockdown MRE11 and ATM, and the lack of effect of Mirin activation of ATM. The extent of shRNA-mediated knockdown of MRE11 and ATM are shown for (A) clones GFP-7F1 and GFP-6D1 and (B) clones EDS-7F2 and EDS-6J8. The extent of knockdown was determined by analyzing the intensity of the ATM and MRE11 bands relative to the intensity of the loading control GAPDH bands (see Table 1). (C) The effect of Mirin on activation of ATM was determined by analysis of phosphorylation of ATM in response to ionizing radiation. Cultures treated with DMSO alone, 20 uM Mirin, or knockdown of ATM were analyzed by western blot 30 min after exposure to 10 Gy of ionizing radiation. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26209132), licensed under a CC-BY licence.

Methylated EDSBs may be repaired by an ATM-dependent pathway. (A) Immunoblots of ATM and DNA-PKcs in ATM shRNA-transfected HeLa cells. GAPDH is included as a loading control. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20356374), licensed under a CC-BY licence.

$Role of HIF-1 alpha , FOXO3 in hypoxia-induced BNIP3 expression. (A) UCB-hMSCs were incubated with various durations of hypoxia (0–48 h). The protein expressions of HIF-1 alpha and beta -actin were detected by western blot. n = 4. (B) UCB-hMSCs were pretreated with NAC (5 mM) for 30 min prior to hypoxia incubation for 24 h. The protein expressions of HIF-1 alpha , lamin A/C and beta -tubulin in non-nuclear and nuclear fractionized cell samples were assessed by using western blot. n = 3. (C) UCB-hMSCs were immuno-stained with HIF-1 alpha and PI (magnification ×600). Scale bars, 37.5 µm. (D) HIF1A siRNA or NT siRNA was transfected to cells prior to hypoxia treatment for 24 h. The mRNA expression of BNIP3 was analyzed by qPCR. n = 6. (E) The protein expressions of BNIP3 and HIF-1 alpha were detected by western blot. n = 4. (F) NAC (5 mM) was pretreated to UCB-hMSCs prior to hypoxia treatment for 24 h. FOXO3, lamin A/C and beta -tubulin proteins expressions were assessed by western blot. n = 3. (G) FOXO3 siRNA transfected to UCB-hMSCs prior to hypoxia treatment for 24 h. The FOXO3 mRNA expression was measured by qPCR. n = 6. (H) BNIP3, FOXO3 and beta -actin expressions were detected by western blot. n = 3. Western blot data were normalized by beta -actin, and qPCR data were normalized by ACTB mRNA expression level. Lamin A/C and beta -tubulin were used as nuclear and non-nuclear protein controls, respectively. Quantitative data are presented as a mean ± S.E.M. All blots and confocal images are representative. *p < 0.05 versus control, #p < 0.05 versus hypoxia. Image collected and cropped by CiteAb from the following open publication (//linkinghub.elsevier.com/retrieve/pii/S2213231717303804), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Pm

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Validated by:

Validated by:

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NB100-104

ATM Antibody

(2 Reviews)

(99 Publications)

0.05 ml

NB100-104

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - GM00637 cells with KU55933 pretreatment (a) were exposed to 50 uM spermidine or CCCP, followed by immunofluorescence analyses of total and p-ATM on Ser-1981. The scale bar is 10 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700) licensed under a CC-BY license.

Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HeLa cells with Dylight 550-conjugated ATM Antibody [NB100-104R] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.

<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer and mammosphere populations. Expression of proteins involved in the NHEJ pathway of DSB repair in response to increasing doses of ionizing radiation. Lysates were prepared from unirradiated cells and from cells harvested one hour after exposure to 1 or 10-Gy 60Co I3-radiation and analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM and phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 and Ser2056, respectively. Actin served as a loading control. Image collected and cropped by Citeab from the following publication (Senescence evasion by MCF-7 human breast tumor-initiating cells. Breast Cancer Res (2010)) licensed under a CC-BY license.

Western Blot: ATM Antibody [NB100-104] - Detection of ATM in Raji whole cell lysate using [NB100-104]. Observed molecular weight ~300 kDa. Theoretical molecular weight 351 kDa.

Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.05% Triton X-100. Then cells were incubated with [NB100-104] at a 1:100 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Flow Cytometry: ATM Antibody [NB100-104] - Analysis of PE conjugate of ATM Antibody [NB100-104PE]. An intracellular stain was performed on HeLa cells with ATM antibody [NB100-104PE] (blue) and a matched isotype control [NBP2-24893PE] (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin.

Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HepG2 cells with PE-conjugated ATM antibody [NB100-104PE] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.

Depletion of SMARCAL1 induces DNA damage and checkpoint activation in iSML1 iPSCs. (C) Immunoblot detection of the indicated DDR proteins in iSML1 iPSCs after 14 days of continuous treatment with DOX. Lamin B1 was used as the loading control. Data are mean+/-s.e.m. from three independent experiments. *P<=0.05, **P<=0.01, ***P<=0.001 (two-way ANOVA test). ns, not significant. Scale bars: 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31515241), licensed under a CC-BY licence.

Osteopontin (OPN) is weakly expressed in NHF, HUVSMC and HUVEC and is not induced in hypoxia. A, Levels of OPN mRNA in AVF patients (n = 12) compared to control veins (Ctl). ****, P < .0001 (Test Mann‐Whitney). B, Representative immunofluorescence of OPN (red staining and arrow) and alpha‐smooth muscle actin ( alpha ‐SMA—green staining and arrows) of human control upper‐arm vein and venous limb of a mature AVF. Osteopontin quantification of group data (vein, n = 3; AVF, n = 2), unpaired t test, P < .01 (right). C, Quantitative immunoblotting to detect recombinant OPN protein. Serial dilutions from 50 to 0.2 ng were used. D, Bone marrow mesenchymal (MSC) and osteoblast (Osteo.) cell lysates analysed by immunoblotting for OPN as indicated. E, LNCap cells were transfected with control siRNA (siCtl), siHIF‐1 alpha (40 nmol/L), siOPN#1 (40 nmol/L) and siOPN#2 (40 nmol/L) and incubated in normoxia (Nx) or hypoxia 1% O2 (Hx) for 48 h. Cell lysates were analysed by immunoblotting for OPN or beta ‐tubulin as indicated. Quantification of the signal to OPN is shown using ImageJ (OPN/ beta ‐tubulin). F–H, NHF (F), HUVSMC (G) and HUVEC (H) cells were transfected with control siRNA (siCtl), siHIF‐1 alpha (40 nmol/L), siHIF‐2 alpha (40 nmol/L) and siHIF1/2 alpha (40 nmol/L + 40 nmol/L), incubated in hypoxia 1% O2 (Hx) for 48 h. AVF, Arteriovenous fistula; HUVEC, human umbilical vein endothelial cells; HUVSMC, Human umbilical vein smooth muscle cells; NHF, normal human fibroblasts Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32032472), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

TRF1HP1 alpha results in reduced TIFs induced by mutant hTR expression. Cells stably expressing TRF1HP1 alpha (WT or mutant variants of HP1 alpha ) were infected with lentivirus containing WT hTR, or mutant hTR (47A or TSQ1) on day 0, selected for stable expression after 48 h, and analyzed on day 5. a Fluorescence microscopy images of representative cells expressing mutant hTR 47A stained with telomeric (Tel-Cy3) peptide nucleic acid (PNA) probes (magenta in merged image) via fluorescent in situ hybridization (FISH), antibody against DNA-damage repair protein marker 53BP1 (green in merged image), and counterstained with DAPI. Zoom-in images (the last row) correspond to yellow-squared regions of the row above. b % TIF per telomere of each nucleus is quantified; n = 94–159 nuclei combining data of three independent experiments. ****p < 0.0001; n.s. (no significance). a, b Scale bar: 10 µm. c Upon TSQ1 expression, TRF1HP1 alpha results in fewer TIFs compared to Vonly, TRF1 or HP1 alpha controls. TRFHP1 alpha ~11.4% shows decreased TIFs compared to Vonly: ~19.7% ***p = 0.0008; TRF1: ~20.4% ***p = 0.0005; HP1 alpha : ~17.9% *p = 0.0137 (n = 30–38 nuclei). b, c Significance is assessed by one-way ANOVA and Dunnett’s multiple comparison test with 95% confidence level. d Fluorescence images of control cells overexpressing WT hTR (n = 27–36 nuclei). Same color scheme as a. TIFs quantification in the presence of e WT hTR or f Vonly (n = 28–36 nuclei) show minimal baseline DNA damage at telomeres. b, c; e, f Error bars represent s.e.m. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30181605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Ma

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB100-104AF405
Alexa Fluor 488	NB100-104AF488
Alexa Fluor 647	NB100-104AF647
Alexa Fluor 700	NB100-104AF700
Biotin	NB100-104B
DyLight 405	NB100-104V
DyLight 488	NB100-104G
DyLight 550	NB100-104R
DyLight 594	NB100-104DL594
DyLight 650	NB100-104C
FITC	NB100-104F
HRP	NB100-104H
PE	NB100-104PE

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NB300-605

iNOS Antibody - BSA Free

(3 Reviews)

(121 Publications)

200uL

NB300-605

Immunohistochemistry-Paraffin: iNOS Antibody [NB300-605] - Immunohistochemistry was performed on normal deparaffinized human Heart tissue.

Immunocytochemistry/Immunofluorescence: iNOS Antibody [NB300-605] - Analysis of iNOS in A549 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a iNOS polyclonal antibody at a dilution of 1:20 overnight at 4C, washed with PBS and incubated with a DyLight 488 conjugated secondary antibody. iNOS staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown.

<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - iNOS in stimulated astrocytes. Western blot image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - LCA-induced oxidative stress in 4T1 breast cancer cells. The 4T1 cells were treated with LCA for 48 h, then the indicated measurements were performed. The level of iNOS protein was detected by western blotting (n = 3). Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/11/9/1255), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: iNOS Antibody [NB300-605] - Analysis of iNOS in NIH-3T3 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a iNOS polyclonal antibody at a dilution of 1:20 overnight at 4C, washed with PBS and incubated with a DyLight 488 conjugated secondary antibody. iNOS staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown.

Indolepropionic acid (IPA) induced oxidative stress, cellular energy stress, and decreased the proportions of cancer stem cells. 500,000 cells/well 4T1 cells were treated with IPA in the concentrations indicated for 24 h; then, (A) lipid peroxidation was measured by TBARS assay, and (B) 4HNE expression was assessed by Western blotting (representative figure, n = 3). In the same cells (C), the protein expression of NRF2 (at 68 kDa) and iNOS were determined by Western blotting (n = 3), while (D) the mRNA expression of catalase (cat) was determined by RT-qPCR (n = 3). (E) The expression of the indicated proteins (pACC, ACC, FOXO1, and PGC-1beta) were determined by Western blotting (n = 3, except for PGC-1beta, where n = 2). (F) 100,000 cells/well 4T1 cells were treated with the indicated concentration of IPA for 24 h; then, the proportions of aldehyde dehydrogenase-positive cells were determined in Aldefluor assays using flow cytometry (n = 3). For Western blots, a typical experiment was displayed. Fold data were log2 transformed to achieve normal distribution. Statistical significance was determined using the ANOVA test followed by Dunnett's post-hoc test, except for panel F, where Student's t-test was used. * and *** indicate statistically significant difference between control and treated samples at p < 0.05 and p < 0.001, respectively. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32854297), licensed under a CC-BY licence.

Inhibitory effect of MMPP on amyloidogenesis and STAT3 translocation in astrocytes and microglia cells. The expression of APP, BACE1 and C99 was detected by Western blotting using specific antibodies in astrocytes (a) and microglia cells (b). Each blot is representative of three experiments. The activity of beta-secretase was investigated using assay kit in astrocytes (c) and microglia cells (d). Values are presented as mean +/- S.D. of the three independent experiments performed in triplicate. #p < 0.05 compared to control, *p < 0.05 compared to LPS. Iba-1, COX-2, and iNOS proteins were detected by Western blotting using specific antibodies in astrocytes (e) and microglia cells (f). NO level was measured in astrocytes (g) and microglia cells (h). Activation of STAT3 was investigated using EMSA in astrocytes (i) microglial cells (j) were determined and the expression of STAT3 and phopho-STAT3 was also detected by Western blotting using specific antibodies (k), (l). For the cropped images, samples were run in the same gels under same experimental conditions and processed in parallel. Each band is representative for three experiments Image collected and cropped by CiteAb from the following publication (//link.springer.com/10.1007/s12017-017-8469-3), licensed under a CC-BY licence.

miR-27a/b prevent pUbS65 accumulation upon mitochondrial damage. a, b Overexpression of PINK1 increased pUbS65 accumulation in HeLa cells only when incubated with CCCP. 48 h post-transfection, cells were incubated with 10 μM CCCP for 2 h and pUbS65 levels were determined by Western blot (n = 3, two-way ANOVA). c, d Overexpression of miR-27a/b inhibited pUbS65 accumulation by CCCP in HeLa cells (n = 4, two-way ANOVA). e, f Inhibition of endogenous miR-27a/b increased pUbS65 accumulation by CCCP in HeLa cells (n = 4, two-way ANOVA). PINK1 levels were normalized to corresponding GAPDH level and quantified as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB300-605AF405
Alexa Fluor 488	NB300-605AF488
Alexa Fluor 647	NB300-605AF647
Alexa Fluor 700	NB300-605AF700
Biotin	NB300-605B
DyLight 350	NB300-605UV
DyLight 405	NB300-605V
DyLight 488	NB300-605G
DyLight 550	NB300-605R
DyLight 594	NB300-605DL594
DyLight 650	NB300-605C
DyLight 680	NB300-605FR
DyLight 755	NB300-605IR
FITC	NB300-605F
HRP	NB300-605H
Janelia Fluor 549	NB300-605JF549
Janelia Fluor 646	NB300-605JF646

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-605SS

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At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat

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Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

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Modification

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Clone

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Species Glossary

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iNOS Antibody - BSA Free