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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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

Sizes:

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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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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NB100-104

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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NB300-144

Laminin Antibody

(9 Reviews)

(122 Publications)

0.1 ml

NB300-144

MxIF analysis of mouse submandibular salivary gland morphogenesis. MxIF of a developmental TMA including embryonic stages (E14, E16, E18) and postnatal stages (P5 and P20) was performed using sequential application of directly conjugated antibodies to detect multiple markers of tissue structures and cell types on the same tissue sections. Tissue compartments. The epithelium, mesenchyme, neurons, and basement membranes was detected using antibodies directed towards E-cadherin (ECAD, red), platelet-derived growth factor (PDGFR, green), beta III tubulin (bIII, magenta), and Laminin Antibody [NB300-144] (LMN, cyan), respectively. Image collected and cropped by CiteAb from the following publication (//bio.biologists.org/cgi/doi/10.1242/bio.20134309), licensed under a CC-BY license.

Staining of mouse section of cortex stained with Laminin Antibody [NB300-144] (red). Blue is DAPI staining of DNA. This antibody reveals strong staining in the basement membranes of blood vessels.

Staining of rat spinal cord and dorsal root paraformaldehyde/paraffin-embedded tissue using Laminin Antibody [NB300-144]. Pepsin antigen retrieval was performed on this tissue sample.

Analysis of rat heart cells lysates (lane 1) and 0.2 ug of purified laminin protein from mouse EHS sarcoma (lane 2) Laminin Antibody [NB300-144] recognizes 3 laminin isotypes: alpha 1 (440 kDa), beta 1 (220 kDa) and gamma 1 (220 kDa). Also recognized is a laminin binding protein at 120 kDa in both rat heart lysates and purified laminin protein. Since this protein always coexpresses with laminin this crossreactivity is irrelevant. Theoretical molecular weight of LAMA1 is 337 kDa.

IF Confocal analysis of HeLa cells using Laminin Antibody [NB300-144] (1:5). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green, A). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red, B). DAPI was used to stain the cell nuclei (blue, C).

Western blot analysis of the effects of IP6, Ins, IP6 + Ins and normal saline on the levels of collagen IV, Laminin and Fibronectin, with Laminin Antibody [NB300-144]. IP6 or Ins treatment decreased the protein expression of LN and FN, and the combined IP6 + Ins treatment resulted in significantly greater effects compared with treatment with either compound alone. The Western blot membranes were stripped and reprobed for beta-actin as an internal control to confirm equal loading. (A) representative blots from one of three separate experiments; (B) relative band intensities based on densitometry. The results are expressed as the mean +/- standard deviation from three independent experiments. * p < 0.05 compared to the IP6 + Ins group; #p < 0.05 compared to the normal saline group. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/8/5/286), licensed under a CC-BY license.

Immunofluorescence staining for extracellular matrix proteins in day 1 and day 7 HWJSC spheroids. HWJSC spheroids were cultured for either 1 day or 7 days (with 6 days of osteogenic differentiation), fixed, and stained for extracellular matrix protein: laminin (C) and counter-staining with Hoechst. Scale bars represent 100 um. Image collected and cropped by CiteAb from the following publication (journals.plos.org/plosone/article?id=10.1371/journal.pone.0184155), licensed under a CC-BY license. Using the Alexa Fluor 488 format of this antibody.

Laminin staining on an E12.5 mouse Right Ventricle. IHC-Fr image submitted by a verified customer review.

A surface stain was performed on HeLa cells with the Alexa Fluor 647 conjugate of Laminin Antibody [NB300-144AF647] (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 2.5 ug/mL for 20 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Analysis of Laminin-1 expression in mouse EHS tumor crude extracts (left) and Laminin-2 expression in rat heart crude extracts (right), using Laminin Antibody [NB300-144]. The Laminin polyclonal antibody was used at 1 ug/mL. Theoretical Molecular Weight of NB300-144 is 337 kDa.

VSOP observed in perivascular-restricted spinal cord lesions with intact BBB. Immunostaining for laminin (brown) using Laminin Antibody [NB300-144] shows vascular endothelium and glia limitans of a perivascular lesion, along with infiltrating cells and VSOP (blue). Image collected and cropped by CiteAb from the following publication (//asn.sagepub.com/lookup/doi/10.1042/AN20120081), licensed under a CC-BY license.

SOX17 regulates adult muscle regeneration after injury in Pax7CreERT2/+;Sox17fl/fl mutant mice. Representative images of cryosections from regenerating adult TA muscles d28 after injury, showing immunofluorescence for PAX7+ (quiescent, arrows) cells. Scale bar, 25 Aum. Image collected and cropped by Citeab from the following publication (SOXF factors regulate murine satellite cell self-renewal and function through inhibition ofI2-catenin activity. Elife (2018)) licensed under a CC-BY license.

VSOP observed in perivascular-restricted spinal cord lesions with intact BBB (B) Immunostaining for laminin (brown) shows vascular endothelium and glia limitans of a perivascular lesion, along with infiltrating cells and VSOP (blue). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23452162), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt, ChHa, In, Ma, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, ChHa, In, Ma, Rb, Sh

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	NB300-144AF350
Alexa Fluor 405	NB300-144AF405
Alexa Fluor 488	NB300-144AF488
Alexa Fluor 532	NB300-144AF532
Alexa Fluor 594	NB300-144AF594
Alexa Fluor 647	NB300-144AF647
Alexa Fluor 700	NB300-144AF700
Alexa Fluor 750	NB300-144AF750
Allophycocyanin	NB300-144APC
Allophycocyanin/Cy7	NB300-144APCCY7
Biotin	NB300-144B
DyLight 350	NB300-144UV
DyLight 405	NB300-144V
DyLight 488	NB300-144G
DyLight 550	NB300-144R
DyLight 594	NB300-144DL594
DyLight 650	NB300-144C
DyLight 680	NB300-144FR
DyLight 755	NB300-144IR
FITC	NB300-144F
HRP	NB300-144H
Janelia Fluor 549	NB300-144JF549
Janelia Fluor 646	NB300-144JF646
PE	NB300-144PE
PE/Atto594	NB300-144PEATT594
PE/Cy5.5	NB300-144PECY55
PE/Cy7	NB300-144PECY7
PerCP	NB300-144PCP
mFluor Violet 450 SE	NB300-144MFV450
mFluor Violet 500 SE	NB300-144MFV500
mFluor Violet 610 SE	NB300-144MFV610

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NB100-56875

GAPDH Antibody

(5 Reviews)

(114 Publications)

0.1 mg

NB100-56875

$Western Blot: GAPDH Antibody [NB100-56875] - Analysis of GAPDH using this antibody at 1:500 in nuclear and cytoplasmic fractions made from Drosophila head extracts. Data courtesy of Dr. Jerry Lin, University of Wisconsin-Madison.$

Western Blot: GAPDH Antibody [NB100-56875] - Analysis using HeLa cells. Theoretical molecular weight: 36 kDa.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 and Rab5. Western blot analysis of control fly head samples fractionated into a cytosolic and membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker and GAPDH as a cytosolic marker. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0170106), licensed under a CC-BY license.$

Western Blot: GAPDH Antibody [NB100-56875] - Particle-induced Changes in Apoptosis are Restored by Firoin. Peripheral blood neutrophils from healthy donors (n57), 2 h pre-treated with indicated amounts of firoin (F) or 1 mM ectoine (E) before CNP exposition (33 mg/ml). : 6 h post CNP-treatment the anti-apoptotic Mcl-1 expression was measured by Western blot analysis. GAPDH was used as a loading control. Two representative blots from different individuals are shown and irrelevant lanes were removed. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0111485), licensed under a CC-BY license.

Simple Western: GAPDH Antibody [NB100-56875] - Lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing A246conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

Particle-induced Changes in Apoptosis are Restored by Firoin.Peripheral blood neutrophils from healthy donors (n = 7), 2 h pre-treated with indicated amounts of firoin (F) or 1 mM ectoine (E) before CNP exposition (33 ug/ml). A: After 16 h of CNP treatment, cells were stained with Annexin V and analysed flow cytometrically. Normalized values of % Annexin V-positive cells are shown. Natural apoptosis of untreated cells was considered as 1. Dark bars, CNP-treated, light bars, untreated. * Significantly different from CNP alone (Mann-Whitney U Test after Bonferroni correction for multiple testing p<0.05). B: 6 h post CNP-treatment the anti-apoptotic Mcl-1 expression was measured by Western blot analysis. GAPDH was used as a loading control. Two representative blots from different individuals are shown and irrelevant lanes were removed. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0111485), licensed under a CC-BY licence.

Analysis of non-canonical inflammasome pathway. D) Western blotting for the cleaved forms of CASP1 (p20), CASP4 (p20), and GSDMD (N-terminal). S: SCGB3A2, N: nigericin. Experiments were repeated more than twice and same results were obtained. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33452234), licensed under a CC-BY licence.

No dystrophin expression was detected in cardiac and skeletal muscles of Dmdmdx rats.(A) Male 7 month-old rats of line 61, wild-type littermate controls (WT) and Dmdmdx were sacrificed and biopsies from tibialis cranialis muscles (TC) and hearts (H) were harvested. Western-blot of total proteins (50 ug) was incubated with NCL-DYS2 and Manex1011C monoclonal antibodies (C-terminal and exons 10/11 epitopes, respectively). This revealed undetectable levels of the 427 kDa dystrophin band in line 61 Dmdmdx rats. Muscle from a GRMD dog (GD) was used as negative control and samples from WT rats were used as positive controls. Staining with an anti-GAPDH polyclonal antibody validated equal protein loadings. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110371), licensed under a CC-BY licence.

Antigen uptake is reduced in K14E7 mice.Epidermal cell suspensions from C57BL/6 and K14E7 mice were cultured with Alexa-555-labelled OVA overnight at 37°C, stained and analysed by flow cytometry (A). The Alexa-555-OVA+ LC (CD45.2+, MHC Class II+, CD207+) as a percentage of total LC (B) and the level of expression of Alexa-555-OVA on the positive stained LC is shown (C). **P < 0.01; *P < 0.05 (Mann-Whitney U test). Confocal imaging of CD207+, MHCII+ LC that have taken up Alexa-555-OVA (D). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0127155), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NB600-633

IL-1 beta/IL-1F2 Antibody

(4 Reviews)

(92 Publications)

0.1 mg

NB600-633

Immunohistochemistry: IL-1 beta/IL-1F2 Antibody [NB600-633] - Analysis of: Human IL1beta antibody Secondary antibody: Peroxidase goat anti-rabbit at 1:10,000 for 45 min at RT Localization: cytoplasm Staining: Close up of medullary lymph node: positive staining in the cytoplasm of circulating macrophages. Neg Ctr (far right) normal rabbit IgG with pH 6.2 40X

Western Blot: IL-1 beta/IL-1F2 Antibody [NB600-633] - Analysis of IL-1 beta in Rhesus fetal membrane using anti-IL-1 beta antibody. Image from verified customer review.

Western Blot: IL-1 beta/IL-1F2 Antibody [NB600-633] - Antibody was used at a 1:200 dilution incubated 1h at room temperature to detect dog IL-1b by Western blot. Lane 1 and 2 were loaded with 2.5 ug and 500 ng of dog IL-1b respectively. The molecular weight of the detected band is estimated by comparison to molecular weight markers (not shown). Detection occurred using a 1:3,000 dilution of IRDye (TM) 800 conjugated Donkey anti-Rabbit IgG for 1h at room temperature.

Western Blot: IL-1 beta/IL-1F2 Antibody [NB600-633] - pro-IL-1beta in glioblastoma cells. Image from verified customer review.

Western Blot: IL-1 beta/IL-1F2 Antibody [NB600-633] - Lane 1: Human IL-1Beta. Load: 5 ng per lane. Primary antibody: Human IL-1Beta antibody at 1:2,000 for overnight at 4C. Secondary antibody: Peroxidase rabbit secondary antibody at 1:40,000 for 30 min at RT. Block: Blocking Buffer for Fluorescent Western Blotting for 30 min at RT. Predicted/Observed size: 17 kDa, 17 kDa for Human IL-1Beta. Other band(s): Unspecific band at 35 kDa.

Western Blot of Rabbit anti-Human IL-1beta antibody. Lane 1: Human IL-1beta. Load: 5 ng per lane. Primary antibody: Human IL-1beta antibody at 1:2,000 for overnight at 4C. Secondary antibody: Peroxidase rabbit secondary antibody at 1:40,000 for 30 min at RT. Block: Blocking Buffer for Fluorescent Western Blotting () for 30 min at RT. Predicted/Observed size: 17 kDa, 17 kDa for Human IL-1beta. Other band(s): Unspecific band at ~35 kDa.

$miR-27a/b prevent Parkin translocation to mitochondria upon mitochondrial damage. a, b 48 h post-transfection, HeLa cells were incubated with 10 μM CCCP for 2 h. After isolating the mitochondria-enriched fractions, Parkin translocation and LC3-II were assessed by Western blot. Each protein level was normalized to corresponding mitochondrial loading control (SOD2) level and quantified as a percentage of control (n = 3, two-way ANOVA). Purity of mitochondrial fraction was assessed by monitoring p38 cytosolic and VDAC1 mitochondrial markers. PN; post-nuclear, C; cytoplasm, M; mitochondrial (A). c, d 48 h post-transfection, HeLa cells stably expressing GFP-Parkin were visualized by GFP, a mitochondrial marker (TOM20) antibody, and a nuclear dye (Hoechst) as indicated. Scale bars correspond to 10 μm. Parkin translocation was quantified as the ratio of cytoplasmic to nuclear GFP signal and the resulting ratios were normalized to control. Data were collected from 4 independent replicates (n > 1000 cells) and are shown as a percentage of control. Values are mean ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Expression of PACAP, VIP, VIPRs, HIF-1 alpha , HIF-2 alpha , and EGFR in glioblastoma multiforme (GBM). (A) Representative immunoblot of PACAP and VIP precursor peptides and PAC1R, VPAC1R, and VPAC2R expression on frozen glioblastoma sample. (B) Representative immunoblot and photomicrographs of signals detected by antibodies direct against HIF-1 alpha , HIF-2 alpha , and EGFR in a frozen glioblastoma sample. Image collected and cropped by CiteAb from the following open publication (//journal.frontiersin.org/Article/10.3389/fphar.2016.00139/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca, Pm, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Pm, SyHa

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Validated by:

Validated by:

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NB600-936

beta Tubulin Antibody - BSA Free

(7 Reviews)

(84 Publications)

0.1 ml

NB600-936

Western Blot: beta Tubulin Antibody [NB600-936] - Analysis of extracts from HeLa, A549 and Jurkat cells using NB600-936 Beta-tubulin antibody at 1:1000

<b>Biological Strategies Validation. </b>Western Blot: beta Tubulin Antibody - BSA Free [NB600-936] - beta Tubulin Antibody [NB600-936] - Reduced levels of NADPH oxidases 1 and 4 at 18% versus 5% O2. (a) Representative Western blots showing Nox1 and Beta-tubulin in PC-3 cells or Nox4 and Beta-tubulin in C2C12 cells, at 5% and 18% O2. (b, c) Average Nox1 signal How Supraphysiological Oxygen Levels in Standard Cell Culture Affect Oxygen-Consuming Reactions. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30363917/) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: beta Tubulin Antibody [NB600-936] - PC12 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-beta Tubulin Antibody (NB600-936) at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunohistochemistry-Paraffin: beta Tubulin Antibody [NB600-936] - Analysis of FFPE tissue section of normal human skin using 1:2000 dilution of beta Tubulin antibody. Intense cytoplasmic staining of beta Tubulin (TUBB) protein was observed in various cells of the epidermal as well as the dermal cells [10X Magnification].

Western Blot: beta Tubulin Antibody [NB600-936] - Analysis in HeLa whole cell lysate at a 1:1,000 dilution.

$Western Blot: beta Tubulin Antibody [NB600-936] - Expression of pluripotency related markers and a sphere culture of BEAS-2B under normoxia. HIF-2alpha expression was detected in the nucleus of BEAS-2B under normoxia by western blotting. Beta tubulin and TATA binding protein (TBP) were used as protein markers for the cytosol and nucleus fraction, respectively. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep29311), licensed under a CC-BY license.$

Immunocytochemistry/Immunofluorescence: beta Tubulin Antibody [NB600-936] - Confocal immunofluorescent analysis of C2C12 cells using beta Tubulin antibody (NB600-936, 1:5). 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).

Immunocytochemistry/Immunofluorescence: beta Tubulin Antibody [NB600-936] - Analysis of beta Tubulin in mouse hippocampal primary culture. Image courtesy of product review by Lin Yi-Wen.

Immunocytochemistry/Immunofluorescence: beta Tubulin Antibody [NB600-936] - NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-beta Tubulin Antibody (NB600-936) at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunohistochemistry-Paraffin: beta Tubulin Antibody [NB600-936] - Analysis of FFPE tissue section of human esophageal squamous cell carcinoma (SCC) using 1:2000 dilution of beta Tubulin antibody. Strong cytoplasmic immuno-positivity of beta Tubulin (TUBB) was observed in SCC cells as well as the associated tumor stromal cells [10X Magnification].

Immunohistochemistry-Paraffin: beta Tubulin Antibody [NB600-936] - Analysis of FFPE tissue section of normal human brain using 1:2000 dilution of beta Tubulin antibody. The various brain cells depicted strong cytoplasmic immunoreactivity of beta Tubulin (TUBB) protein [10X Magnification].

Expression of AAV transgene before and after experimental autoimmune uveoretinitis (EAU) induction. (B) Western blot from retinas harvested 14 days after IRBP immunization. Membrane was probed with anti-GFP and anti-Tubulin antibodies. Image shows expression of sGFP on both sGFP and sGFP-TatM013v5 retina lysates. (n = 2-3 retina samples from different mice per group). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31795515), licensed under a CC-BY licence.

EBNA1 expression is associated with upregulation of MTH1 and oxidative damage repair pathways. The expression of MTH1, OGG1, and MUTYH was investigated by western blots and qPCR in BJAB-tTAE1 cells upon addition and withdrawal of doxycycline. a Representative western blots illustrating the correlation between the reversible down- and upregulation of MTH1 and EBNA1 in BJAB-tTAE1 cells upon addition and withdrawal of doxycycline. GAPDH was used as loading control. b Densitometry quantification of MTH1 and EBNA1 expression in BJAB-tTAE1 cells. The mean intensity of the MTH1 and EBNA1 specific bands relative to GAPDH in three independent experiments is shown in the figure. c Regression analysis of the relationship between expression levels of MTH1 and EBNA1. The data from three independent experiments were used for the plot. d Representative western blots illustrating the expression of MTH1, MUTYH, and OGG1 in BJAB-tTAE1 cells cultured for two weeks in the presence or absence of doxycycline. e Fold change is the ratio between the intensity of the specific band in cells cultured without or with doxycycline. The mean ± SD of four independent experiments is shown. f qPCR analysis of the levels of MTH1, OGG1, and MUTYH transcripts in BJAB-tTAE1 cells cultured for 2 weeks in the presence or absence of doxycycline. The mean ± SE of the fold change in six independent experiments each performed in triplicate is shown Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Characterization of immunosorted NCAM1+ subpopulationA. RT-PCR analysis of gene expression in NCAM1 cell fractions. GAPDH was used as endogenous control and NCAM1− cell were used as the calibrator sample for RQ calculation (therefore = 1). Data were analysed using SDS 3.2 software and presented as average RQ ± SDEV of three replicates. ***p < 0.001, *p < 0.05 versus NCAM1−.B–D. Immunofluorescence staining of NCAM1+ and NCAM1− subpopulations for E-cadherin (E-cad) (B, red) vimentin (C, green) and SIX2 (D, green). Nuclei stained with Dapi (blue). (B–C) Images were obtained using Olympus DP72 camera attached to Olympus BX51 fluorescence microscope and processed via cellSens standard software, bar represents 200 μm. (D) Images were obtained using Zeiss LSM 510 confocal microscope, bar represents 50 μm.E. Fluorescent quantification of SIX2 immunostaining as represented in (D).F. Double labelling of sorted NCAM1+ cells for NCAM1 and SIX2: NCAM1 with DAPI (upper panel; red and blue channels), NCAM1 with SIX2 (lower panel; red and green channels), indicating both NCAM1+ SIX2+ (arrows) and NCAM1+ SIX2− (arrowheads) cells.G. Graph represents percentage of NCAM1+ SIX2+ cells and NCAM1+ SIX2− cells.H. Clonogenic efficiency of NCAM1+ cells sorted from hFK and cultured in SFM. Data are presented as average CE(%) ± SDEV. **p < 0.01 versus NCAM1−.I. Representative morphology of NCAM1+ and NCAM1− clones. Cells were observed using a Nikon Digital Sight camera attached to a Nikon Eclipse TS100 microscope.J. Clonogenic capacity of hFK cells treated with IMGN901(ADC 55 nM), huN901 (Ab55 nM) or not treated (control). Data are presented as average CE(%) ± SDEV. ***p < 0.001, *p < 0.05 versus control group. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23996934), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

PGE1 induces HIF-1 alpha protein accumulation in vascular-derived cells.Human aortic smooth muscle cells (HASMCs) (A and B), human umbilical vein endothelial cells (HUVECs) (C and D), and HEK293 cells (G) were exposed to 1 or 10 µM PGE1 under 20% O2 or 1% O2 conditions for 4 h. After treatment, cells were harvested and whole-cell lysates were subjected to immunoblot assay for HIF-1 alpha , HIF-1 beta , and beta -actin protein expression. Experiments were repeated thrice (A, C and G). Representative immunoblots are shown (A and C). Band intensities were analyzed densitometrically (B and D). Fold induction relative to lane 1 was plotted as mean ± S.D. ∗P < 0.05 compared with the control. HASMCs (E) and HUVECs (F) were exposed to 1 µM PGE1 for the indicated times under 20% O2 and were harvested for immunoblot assay for HIF-1 alpha protein. Experiments were repeated twice. Representative immunoblots are shown. (H) HASMCs and HUVECs were exposed to 10 µM PGE1 for 4 h under 20% O2 and were harvested for immunoblot assay for HIF-2 alpha protein. Experiments were repeated twice. Representative immunoblots are shown. I. HASMCs were exposed to 1 µM PGE1, lipo-PGE1 and PGE1-alfadex under 20% O2 conditions for 4 h. After treatment, cells were harvested and whole-cell lysates were subjected to immunoblot assay for HIF-1 alpha . Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24349900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

TIP30 was regulated by HIF-2 alpha at protein level in HCC cell lines. Lentivirus infection was used to establish a stable knocking-down or overexpression of HIF-2 alpha in MHCC97H cell lines. The relationship between HIF-2 alpha and TIP30 was detected by Western blot. a Knocking-down of HIF-2 alpha upregulated TIP30 expression. b Knocking-down of TIP30 did not influence the expression of HIF-2 alpha . c, d Metformin in combination with sorafenib synergistically inhibited HIF-2 alpha protein expression and subsequently upregulated TIP30 protein expression. e MHCC97H cells were exposed to CoCl2 (400 μM) for 6 h, and anti-HIF-2 alpha or anti-IgG was used for immunoprecipitation. Immunoprecipitated and purified DNA together with 1 % of input DNA were used for PCR amplification of a 214-bp product encompassing HRE region of TIP30 promoter Image collected and cropped by CiteAb from the following open publication (//www.jhoonline.org/content/9/1/20), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ATM and NF-kappa B activation are downregulated in Ercc1-/ delta mice heterozygous for Atm. (A) Livers were collected at 12 weeks of age from WT, Ercc1-/ delta and Ercc1-/ delta Atm+/- mic (n=3 per genotype) and lysates analyzed by western blot for activation of ATM and its downstream effectors. (B) Same liver lysates were used to measure phosphorylation of p65 and I kappa B alpha . (C) Western blot analysis of livers from 16-week-old WT, Ercc1-/ delta and Ercc1-/ delta Atm+/-mice (n=3 per genotype) probed for activation of ATM. GAPDH was used as a loading control. (D) Same liver lysates used to measure activation of NF-kappa B. (E) Fourteen-week-old livers from Ercc1-/ delta and Ercc1-/ delta p65+/- mice (n=3 per genotype) were analyzed by western blot for activation of ATM (F) and NF-kappa B. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32201398), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Expression of the mitochondrial biogenesis proteins: SIRT1, PGC1 alpha , TFAM and SIRT3 in H1299, H1299r, P31 and P31r cell lysates as determined by immunoblot analysisWhole cell lysates were prepared from confluent cultures of H1299, H1299r, P31 and P31r cells. Proteins (90 μg) were resolved in 10% SDS-PAGE gels and transferred to a PVDF membrane. Blots were probed for SIRT1, PGC1 alpha , TFAM and SIRT3 or the loading control gamma -tubulin. Figure shows representative blots of (A) of SIRT1, (B) PGC1 alpha , (C) SIRT3, (D) TFAM protein expression; each from three independent experiments. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.21885), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ce, Ch, ChHa, I, In, Pm, Xp, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ce, Ch, ChHa, I, In, Pm, Xp, Ze

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	NB600-936AF350
Alexa Fluor 405	NB600-936AF405
Alexa Fluor 488	NB600-936AF488
Alexa Fluor 532	NB600-936AF532
Alexa Fluor 594	NB600-936AF594
Alexa Fluor 647	NB600-936AF647
Alexa Fluor 700	NB600-936AF700
Alexa Fluor 750	NB600-936AF750
Allophycocyanin	NB600-936APC
Biotin	NB600-936B
DyLight 350	NB600-936UV
DyLight 405	NB600-936V
DyLight 488	NB600-936G
DyLight 550	NB600-936R
DyLight 594	NB600-936DL594
DyLight 650	NB600-936C
DyLight 680	NB600-936FR
DyLight 755	NB600-936IR
FITC	NB600-936F
HRP	NB600-936H
Janelia Fluor 549	NB600-936JF549
Janelia Fluor 646	NB600-936JF646
PE	NB600-936PE
PerCP	NB600-936PCP
mFluor Violet 450 SE	NB600-936MFV450
mFluor Violet 500 SE	NB600-936MFV500
mFluor Violet 610 SE	NB600-936MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB600-936SS

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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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Protein/Target

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Reactivity

Citation

Antibody Validation

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Species Glossary

HIF-2 alpha/EPAS1 Antibody - BSA Free

Survivin Antibody - BSA Free

IRE1 alpha [p Ser724] Antibody - BSA Free

ATG5 Antibody - BSA Free

NLRP3/NALP3 Antibody - BSA Free

Beclin 1 Antibody - BSA Free

ATM Antibody

iNOS Antibody - BSA Free

Laminin Antibody

GAPDH Antibody

IL-1 beta/IL-1F2 Antibody

beta Tubulin Antibody - BSA Free