Product Search for novus: Novus Biologicals

NB100-2220

LC3B Antibody - BSA Free

(51 Reviews)

(1669 Publications)

0.1 ml

NB100-2220

Lysates of HeLa parental cell line and LC3B knockout HeLa cell line (KO) untreated (-) or treated (+) with 50 uM CQ for 18 hours. PVDF (Polyvinylidene difluoride) membrane was probed with 0.5 ug/mL of Rabbit Anti-LC3B Polyclonal Antibody (Catalog # NB100-2220) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog# HAF008). A specific band was detected for LC3B at a molecular weight of approximately 15 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. GAPDH is shown as a loading control. This experiment was conducted under reducing conditions.

<b>Genetic Strategies Validation. </b>LC3B was detected in immersion fixed CQ treated HeLa cells (left) but was not detected in LC3B knockout HeLa cells (right) using rabbit anti-human LC3B polyclonal antibody (Catalog #NB100-2220) at 0.3 ug/mL for 3 hours at room temperature. Cells were stained using the NorthernLights(TM) 557-conjugated anti-Rabbit IgG Secondary Antibody (red; Catalog # NL004) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm.

<b>Biological Strategies Validation. </b>Contribution of autophagy to lipid droplet formation in WT and KO NSC34 cells.(A) WT and KO NSC 34 cells were treated with (+) or without (-) bafilomycin A (bafA) under basal or HBSS starvation conditions for 4 h and blotted for p62, LC3, and GAPDH. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32321733) licensed under a CC-BY license.

TMEM16A inhibited AngII-induced autophagy in aortas. (D) Representative immunofluorescence staining of LC3 (green) and a-SMA (red) in aortas. Scale bars, 20 um. Quantification of LC3B puncta. Five random fields (2,500 um2/filed) were measured in one section. **P < 0.01 vs. sham + TMcon; ##P < 0.01 vs. AngII + TMcon, one-way ANOVA. n = 14 sections from seven mice per group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32226533) licensed under a CC-BY license.

LC3 accumulation in muscle fibers from patients with PAD (row B - E). Normal fibers from a Non-PAD sample (row A). Scale bar = 100 uM. Image from verified customer review.

Localization of LC3 by immunohistochemical method. The immunohistochemical staining shows that LC3, CRF, and HIF-1alpha have an overlapping localization in villous and extravillous trophoblast. d: decidua; v: villi; DeVe: decidual vessel. Original magnification 40x. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2013/689768/) licensed under a CC-BY license.

Detection of LC3B in mouse ES cell lysates using Rabbit anti- [Catalog # NB100-2220]. LC3 detected at a molecular weight of approximately 17 kDa. Atg5-/- ES cells from Dr. Noboru Mizushima [Mizushima, N. et al. J. Cell Biol. 152 (2001)] Photo courtesy of Dr. Beth Levine, UT SW Medical Center.

ORP1L and VAP-A form cholesterol-dependent ER-AV contact sites MelJuSo cells expressing GFP or GFP-tagged ORP1L mutants were fixed and stained for LC3 and Calnexin. Y477 and D478 in the FFAT motif were mutated to alanines in the ORP1L ydaa mutant. Scale bar, 10 um. Right: co-immunoprecipitation for ORP1L (mutants) with VAP-A. GFP-ORP1L mutants or GFP were isolated from lysates of HEK293T cells co-overexpressing HA-VAPA using GFP-Trap beads. Western blot filters were probed for isolated GFP-tagged proteins, the associated HA-VAP-A and the input HA-VAP-A, as indicated. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms11808), licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Lysates of mouse NIH3T3 and rat PC-12 cell lines untreated (-) or treated (+) with CQ. PVDF (Polyvinylidene difluoride) membrane was probed with 0.5 ug/mL rabbit anti-LC3B polyclonal Antibody (Catalog # NB100-2220, Novus Biologicals), followed by 1:2000 dilution of goat anti-rabbit IgG secondary antibody. LC3 detected at a molecular weight of approximately 15 kDa in treated NIH3T3 and PC-12 cells.

<b>Biological Strategies Validation. </b>Detection of LC3I and LC3II in mouse cochlea cell line SV-K1 using Rabbit anti- [Catalog # NB100-2220]. Cells were treated with CQ (1 uM), and As2O3 (1 uM) for 24 hrs. Image from verified customer review.

Autophagy Investigation. (A) Representative WBs (Western Blots) of LC3B-I, LC3B-II and GAPDH loading control in DANs derived from 4 iPD patients and 4 healthy controls. (B) WBs from three independent experiments were quantified by densitometry and LC3B-II normalized to a loading control. Grouping of data by healthy vs iPD as well as iPD stratified for T/T and C/C genotype. (C) Ratio of LC3B-II (normalized to loading control) following bafilomycin treatment/untreated. Citation: Marrone L, Bus C, Schondorf D, Fitzgerald JC, Kubler M, Schmid B, et al. (2018) Generation of iPSCs carrying a common LRRK2 risk allele for in vitro modeling of idiopathic Parkinson's disease. PLoS ONE 13(3): e0192497. //doi.org/10.1371/journal.pone.0192497

<b>Biological Strategies Validation. </b>Expression of autophagic protein LC3 in BME-UV1 cells forming acinar structures on Matrigel. Representative images of Western blot analysis of LC3 in bovine MECs grown in 3D culture for 3, 6, 9, and 14 days in differentiation medium (control), enriched with 17beta-estradiol (E2, 1 nM), progesterone (P4, 5 ng/mL), or both (E + P); expression of beta-actin was used as a loading control; graphs below the images show the results of densitometric analysis, in which IOD of each band was measured, and the values were normalized to IOD of beta-actin; the IOD results are presented as means +/- SEM from at least three separate experiments. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2014/382653/) licensed under a CC-BY license.

GNA triggers the formation of autophagic markers in A549 and HeLa cell. Effects of GNA on LC3 protein. A549 cells were treated with various concentrations of GNA for 24 hours or 3 uM GNA for the indicated periods of time, then analyzed by western blotting using anti-LC3 antibodies. GAPDH protein was used as the loading control. The bar graph shows the band intensities of LC3-II relative to those of GAPDH. Mean+/- SEM, n = 3, *means p<0.05, ** p<0.01, one-way ANOVA. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0083604), licensed under a CC-BY license.

Autophagosomes accumulate in neurons of the VH gray matter at day 1 after SCI. Representative images of IHC staining for LC3 (green) and neuronal marker NeuN (red) in VH of gray matter from sham and SCI animals. Stronger co-localization between NeuN and LC3 is apparent at day 1 after SCI. Scale bar is 20 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014527) licensed under a CC-BY license.

Autophagosomes accumulate in microglia and oligodendrocytes of the dorsal white matter adjacent to injury after SCI. Representative images of IHC staining for LC3 (green) and activated microglia marker CD11B (red) in dorsal white matter of sham and SCI animals. Increased co-localization between LC3 and CD11B is apparent at day 1 after SCI. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014527) licensed under a CC-BY license.

Staining of rat brain tissue section. Analysis using Rabbit anti-LC3B Antibody [Catalog # NB100-2220]. Image from verified customer review.

Human ovarian Cancer tissue stained using heat mediated antigen retrieval in pH 6.0 citrate buffer at 1:200 dilution. Image provided by verified customer review.

FFPE (Formalin-Fixed Paraffin-Embedded) tissue section of mouse brain using 1:200 dilution of Rabbit anti-LC3B antibody [Catalog # NB100-2220]. The specific signal of LC3 was detected using HRP-conjugated secondary antibody with DAB (3, 3 -diaminobenzidine) reagent, and nuclei of cells were counterstained using hematoxylin. This LC3B antibody generated a low to moderate levels of cytoplasmic staining in the glial cells. The neurons depicted a moderate to strong staining for LC3 in their cytoplasm.

Analysis using the Biotin conjugate of Rabbit anti-LC3B Antibody [Catalog # NB100-2220]. Staining of brain, cerebral cortex, neurons with cell processes.

SCI leads to lysosomal dysfunction. Representative high magnification images ( x 60) of LC3 (green) and CTSD (red) staining in VH of gray matter from sham and day 1 SCI animals. Decrease in number and intensity of CTSD puncta (lysosomes) and increase in LC3 puncta (autophagosomes) is apparent after SCI. Scale bar is 10 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014527) licensed under a CC-BY license.

Image shows a specific band for LC3B at a molecular weight of approximately 15 kDa in 0.5 mg/mL of Neuro2A lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

LILRB2 antagonism effects on the bactericidal function of the MDSCs are independent of autophagy. (B) Lysates of cells from panel A were collected at 18 h and analyzed using Western blot for the autophagy marker, microtublue-associated light chain-3 (LC3). Lipidation is indicated by LC3-II. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35757769), licensed under a CC-BY licence.

$CQ-induced autophagy inhibition leads to Nrf2 pathway activation in C2C12 muscle cells. a. Treatment of differentiated C2C12 myotubes with autophagy inhibitor CQ increased the sarcoplasmic level of LC3-II and SQSTM1 proteins in a dose- and time-dependent manner, indicating effective inhibition of the autophagic flux. Autophagy inhibition was accompanied by a slight decrease in the sarcoplasmic level of the soluble Keap1 protein (possibly reflecting its sequestration into insoluble protein aggregates) and an increase in the nuclear level of Nrf2 protein. GAPDH and lamin B were used as loading controls for sarcoplasmic and nuclear protein-enriched fractions, respectively; a representative of 3 independent experiments is shown. Image collected and cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/s40478-016-0384-6), licensed under a CC-BY licence.$

Accumulation of an autophagosome marker in the presynaptic terminals of NMJs of SOD1G93A mice (A) Representative confocal micrographs of immunohistochemistry showing accumulation of the autophagosome marker LC3 (grayscale in left panels, green in right panels) in presynaptic terminals of diaphragm NMJs in SOD1G93A mice at P120, but not at NMJs of wild-type mice at P140. Nerves were stained using anti-neurofilament and anti-SV2 antibodies (blue), and postsynaptic acetylcholine receptors were labeled with Alexa 594-conjugated alpha-bungarotoxin (red). In these cross-section images of NMJs, presynaptic terminals are above the bungarotoxin signal, and postsynaptic myotubes are below the bungarotoxin signal. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28890682), licensed under a CC-BY licence.

CAIX expression in PDAC and association with outcomeA. Representative images of immunohistochemical staining showing: negative expression of CAIX in both tumor cell and stromal compartments (top left), positive expression of CAIX in tumor cells but not stromal compartment (top right), positive expression of CAIX in stromal compartment but not tumor cells (bottom left), positive expression of CAIX in both tumor cell and stromal compartments (bottom right). B. Kaplan-Meier analysis of CAIX expression in the distinct tumor cell and stromal compartments and the associated overall survival. C. Representative images of immunohistochemical staining showing low stromal volume and high stromal volume and low and high microvessel density D. Representative images of immunohistochemical staining showing: positive expression of MCT4 in tumor cell compartment and positive expression of MCT4 in tumor stromal compartment. Kaplan-Meier analysis of combinatorial MCT4 and CAIX expression in the stromal compartment and the associated overall survival. Hazard ratios and p-values for each comparison are summarized in the table. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27623078), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Al, Av, Ba, Bv, Ca, Ch, ChHa, Gp, Ha, In, Pm, Pm, Rb, SyHa, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Al, Av, Ba, Bv, Ca, Ch, ChHa, Gp, Ha, In, Pm, Pm, Rb, SyHa, 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	NB100-2220AF350
Alexa Fluor 405	NB100-2220AF405
Alexa Fluor 488	NB100-2220AF488
Alexa Fluor 532	NB100-2220AF532
Alexa Fluor 594	NB100-2220AF594
Alexa Fluor 647	NB100-2220AF647
Alexa Fluor 700	NB100-2220AF700
Alexa Fluor 750	NB100-2220AF750
Allophycocyanin	NB100-2220APC
Biotin	NB100-2220B
DyLight 350	NB100-2220UV
DyLight 405	NB100-2220V
DyLight 488	NB100-2220G
DyLight 550	NB100-2220R
DyLight 594	NB100-2220DL594
DyLight 650	NB100-2220C
DyLight 680	NB100-2220FR
DyLight 755	NB100-2220IR
FITC	NB100-2220F
HRP	NB100-2220H
Janelia Fluor 549	NB100-2220JF549
Janelia Fluor 646	NB100-2220JF646
PE	NB100-2220PE
PerCP	NB100-2220PCP
mFluor Violet 450 SE	NB100-2220MFV450
mFluor Violet 500 SE	NB100-2220MFV500
mFluor Violet 610 SE	NB100-2220MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-2220SS

compare

(select up to 3 products from this page to compare)

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

compare

(select up to 3 products from this page to compare)

NB600-408

Collagen I Antibody

(16 Reviews)

(298 Publications)

0.1 mg

NB600-408

Rat colon tissue stained with Collagen I antibody (red) and Hoechst (blue). IHC-P image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Myofibroblast differentiation requires CD271/NGF activation. Representative alphaSMA (red) and COLLAGEN 1 (red) immunostaining with DAPI (blue) in non-treated (control), TGFbeta-treated cells with or without gamma-secretase inhibitor. Scale bars: 50 um Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-019-09992-3) licensed under a CC-BY license.

Lane 1: Human Collagen Type 1. Lane 2: None. Load: 50 ng per lane. Primary antibody: Collagen Type I antibody at 1:1000 overnight at 4C. Secondary antibody: DyLight 649 rabbit secondary antibody at 1:20000 for 30 min at RT. Block: incubated with blocking buffer for 30 min at RT. Predicted/Observed size: 139 & 130 kDa, 139 & 130 kDa for Collagen Type I. Other Band(s): Collagen Type I splice variants and isoforms.

Representative Western blot image for Collagen I, Collagen 2 and GAPDH. N/group = 8. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.12367) licensed under a CC-BY license.

Macro- and micro-architecture of human adipose tissue lobule. Representative immunostaining of the human AT lobule with Collagen I (COL1), CD34, and DAPI. The position of the septa is underlined, scale bar: 100 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-019-09992-3) licensed under a CC-BY license.

Primary human cardiac fibroblast cells were stained with anti-Collagen I antibody. Cells were cultured for 3 days in DMEM with 10% fetal calf serum. ICC/IF image submitted by a verified customer review.

Cell lysate from human trabecular meshwork. Antibody at 1:1.000. WB image submitted by a verified customer review.

Patient-derived CAF and NF CDMs are architecturally and functionally distinct. (e) Collagen I (red) and fibronectin (blue) staining of patient #1 and #3 NF and CAF CDM. Scale bar, 20 μm. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms12237) licensed under a CC-BY license.

Staining of human HaCaT-ras A5-RT3 (SCC) frozen tumor sections. Image provided by Dr. Wa'el Al Rawashdeh of RWTH Aachen University.

Livers were harvested at 9 wpi, formalin-fixed, and then cryosectioned and stained for markers of inflammation and liver fibrosis. Maximum intensity projections of 12-17 um thick liver sections with immunofluorescently labeled nuclei (DAPI white) alpha-smooth muscle actin NBP2-34760APC (yellow), CD45 (red) and Collagen I NB600-408 (top) or Collagen III/COL3A1 NB600-594 (bottom) (blue) in the liver of uninfected or 9 wpi WT mice. Scale bars represent 50 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32973293/) licensed under a CC-BY license.

Analysis in porcine burn wound lysate using anti-Collagen I alpha 1 antibody. WB image submitted by a verified customer review.

Detection of collagen I in Wistar rat hepatic stellate cells (HSC) in control (GFP-transduced) (left lane) and PPARg-transduced cell lysates (right lane). Protein staining shown below each blot depicts equal protein loading. An equal amount of the whole cell protein (100 ug) was separated by SDS-PAGE and electroblotted to nitro-cellulose membranes. Proteins were detected by incubating the membrane with anti-Collagen I antibody at a concentration of 0.2-2 ug/10 mL in TBS (100 mM Tris-HCl, 0.15 M NaCl, pH 7.4) with 5% non-fat milk. Detection occurred by incubation with a HRP conjugated secondary antibody at 1 ug/10 mL. Proteins were detected by a chemiluminescent method using the PIERCE ECL kit (Amersham Biosciences).

Balb/3T3 mouse embryonic fibroblast cell line stained with Collagen I antibody. IHC-P image submitted by a verified customer review.

Mouse pancreas tissue stained with Collagen I antibody. IHC-P image submitted by a verified customer review.

Human lung tissue section stained with Collagen I antibody at 1:400.

FFPE right lobe of the liver tissue section. A:Central Vein (CV) fibrosis, B: Non-fibrotic CV, C: Perisinusodial fibrosis, D: Non-fibrotic area, E: Protat tract fibrosis, F: Septal fibrosis (arrow). Antigen retrieval: not required. Primary antibody: Anti-collagen type I at 1:1250 for 4C for 24hr. Secondary antibody: Peroxidase biotin-streptavidin rabbit secondary antibody at 1:10,000 for 45 min at RT. Localization: Anti-collagen type I is intra and extracellular. Staining: 3.3'-diaminobenzidine tetrahydrochloride was used as the chromogen. Nuclei were counterstained purple with hematoxylin.

Analysis of FFPE human lung. Primary antibody: Collagen I 1:400. Secondary antibody: Peroxidase goat anti-rabbit at 1:10,000 for 45 min at RT. Localization: Strong staining was observed in the extracellular matrix of the lung. Epithelial cells were negative. Staining: antibody as precipitated red signal with a hematoxylin purple nuclear counterstain.

Analysis of HRP conjugate of NB600-408. FFPE Human Skin at pH 6. Primary antibody: Collagen Type I antibody at 10 ug/mL for 1 h at RT. Localization: Collagen Type I is secreted in the extracellular matrix.

Analysis of HRP conjugate of NB600-408. FFPE Human Skin tissue at pH9. Primary antibody: Collagen Type I antibody at 10 ug/mL for 1 h at RT. Localization: Collagen Type I is secreted in the extracellular matrix. Staining: Collagen Type I as precipitated brown signal (A) with hematoxylin purple nuclear counterstain. With corresponding negative conrol (B).

Imaging of rat calvarial defect bone. IHC-P image submitted by a verified customer review.

Immunohistological staining of EG treated rat kidneys for Collagen. Magnification X40, Scale bar 100 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0185009), licensed under a CC-BY license.

Analysis of Collagen I Antibody on alcohol-fixed rat lung tissue. Primary antibody dilution 1:200. Image from verified customer review.

Immunohistochemistry of Collagen I antibody. Tissue: human lung. Fixation: formalin fixed paraffin embedded. Antigen retrieval: user optimized. Primary antibody: Collagen 1 1:400 Secondary antibody: Peroxidase goat anti-rabbit at 1:10,000 for 45 min at RT. Localization: Strong staining was observed in the extracellular matrix of the lung. Epithelial cells were negative. Staining: antibody as precipitated red signal with a hematoxylin purple nuclear counterstain.

Immunohistochemistry of Rabbit Anti-collagen type I antibody. Tissue: right lobe of the liver section. A:Central Vein (CV) fibrosis, B: Non-fibrotic CV, C: Perisinusodial fibrosis, D: Non-fibrotic area, E: Protat tract fibrosis, F: Septal fibrosis (arrow). Fixation: formalin fixed paraffin embedded. Antigen retrieval: not required. Primary antibody: Anti-collagen type I at 1:1250 for 4C for 24hr. Secondary antibody: Peroxidase biotin-streptavidin rabbit secondary antibody at 1:10,000 for 45 min at RT. Localization: Anti-collagen type I is intra and extracellular. Staining: 3.3'-diaminobenzidine tetrahydrochloride was used as the chromogen. Nuclei were counterstained purple with hematoxylin.

Immunohistochemistry-Paraffin: Rabbit Polyclonal Collagen I Antibody [NB600-408] - Collagen I was stained in human FFPE tissue. Primary antibody dilution: 1/1000 in blocking buffer. HIER antigen retrieval at pH 9 for 20min. AF750 conjugated version of the antibody was used (Catalog # NB600-408AF750). Image from a verified customer review.

Effects of fasudil treatment on tumor stroma in KPC mice.A) Pancreatic tumor tissues from vehicle, gemcitabine, or combination of gemcitabine plus fasudil treated KPC mice were harvested and stained for various stromal markers. Representative images are shown of H&E staining, alpha -SMA, Desmin, CD31, Collagen I, and Movat's pentachrome staining.

Western blot analysis. Comparison of collagen 1 (A and B) and collagen 2 (D and E) among the anterior horn, the body and the posterior horn: (A and D) young model; (B and E) adult model. Comparison of collagen 1 (C) and collagen 2 (F) content between the young and the adult specimens. Values with different superscripts differ for P 50 cells. G, histograms show the rate of colony formation. Data represent the average of three experiments (mean ± SD). **P < 0.01, compared to DMSO treated cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25204354), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Phd2 deletion leads to activation of the Akt–mTOR pathway. a RPPA analysis of tumors with homozygous deletion of Phd2. Tumor tissues from Tyr::CreER; BRafV600E; Phd2−/− or Tyr::CreER; BRafV600E mice were processed and analyzed by RPPA assays. The analyses identified proteins that were significantly changed in mouse melanomas compared to nevi. b Activation of Akt–mTOR pathway after phd2 deletion. Tumor tissues were processed and western blots showed stabilization of HIF-1 alpha and HIF-2 alpha proteins after Phd2 depletion. Increased phosphorylation of Akt, 4EBP1 and S6K was observed in tumors from Tyr::CreER; BRafV600E; Phd2−/− compared with those of Tyr::CreER; BRafV600E mice. c Re-expression of Phd2 inhibits the Akt–mTOR pathway. A BRafV600E; Phd2−/− mouse melanoma cell line was established from melanomas in Tyr::CreER; BRafCA; Phd2lox/lox mice. Phd2 was ectopically reintroduced in these tumor cells. Western blot analysis showed that degradation of HIF-1 alpha and HIF-2 alpha proteins with decreased expression of VEGFR2 decreased phosphorylation of Akt, 4EBP1 and S6K. d Pharmacological inhibition (FM19G11) of HIF pathway in BRafV600E; Phd2−/− melanoma cells. A similar but more pronounced inhibition of the Akt–mTOR pathway was observed using the HIF inhibitor. beta -Actin was used as a loading control. Results are representative of three independent experiments Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30575721), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Aberrant HIF1 alpha expression in PDAC cancer associated fibroblastsA. The level of MCT4 was determined in the indicated established pancreatic cancer cell lines and CAF cultures by immunoblotting. B. The level of MCT1 was determined in the indicated established pancreatic cancer cell lines and CAF cultures by immunoblotting. C. HIF alpha and MCT4 levels were determined by immunoblotting following the knockdown of HIF1 alpha with RNAi or the induction of hypoxia through the use of CoCl2. D. The stability of HIF1 alpha was evaluated in CAFs following treatment with cycloheximide. E. HIF1 alpha was detected by immunoblotting in the presence of cycloheximide in the absence or presence of the proteasome inhibitor MG132. F. HIF1 alpha protein levels were determined in the absence and presence of DMOG. G. RNA levels of the indicated genes as determined by microarray analyses (**p < 0.01 for tumor cell line vs. CAF). H. MG132 was used to interrogate the synthetic rate of HIF1 alpha protein in the indicated cell lines. I. The expression of HIF1 alpha target genes was evaluated in the indicated cell lines by microarray analysis (**p < 0.01 for tumor cell vs. CAF). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27623078), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Chromatin opening activates DDR via a mechanism that requires catalytically functional LOXL2 but can be independent of DNA damage. a gamma -H2AX and 53BP1 staining and foci quantification are shown by immunofluorescence with a specific antibody for gamma -H2AX (left image) or for 53BP1 (right image). Dot graphs indicate the number of foci for gamma -H2AX (upper graph) and 53BP1 (lower graph) per cell in control and LOXL2 KD conditions. b gamma -H2AX staining and foci quantification are shown by immunofluorescence with the indicated antibody after LOXL2 reinfection. MDA-MB-231 cells were first infected with control or LOXL2 KD lentivirus and then, after puromycin selection, again with GFP (MOCKGFP+), wild-type LOXL2-IRES-GFP (LOXL2GFP+), or LOXL2mut-IRES-GFP (LOXL2mutGFP+). Cells were fixed after 24 h. Dot graphs indicate the number of gamma -H2AX foci per GFP-positive cells containing MOCKGFP+ (upper graph), LOXL2GFP+ (middle graph), or LOXL2mutGFP+ (lower graph). c Dot graphs indicate the number of gamma -H2AX (upper graph) and 53BP1 (lower graph) foci per cell in control and LOXL2 KD cells after treatment with 200 μM cordycepin for the indicated timepoints. d gamma -H2AX and 53BP1 staining and foci quantification are shown after immunofluorescence with the indicated antibodies in non-replicative conditions. Dot graphs indicate the number of the gamma -H2AX (left graph) and 53BP1 (right graph) foci in control and LOXL2 KD cells. e Representative image showing DNA damage in control or LOXL2 KD MDA-MB-231 cells, visualized by the alkaline comet assay. Cells were treated with 0.3 μM doxorubicin for 24 h. The graph shows the percentage of MDA-MB-231 positive cells. f Chromosome alterations in control and LOXL2 KD MDA-MB-231 cells. Error bars indicate the SD from at least three independent experiments. *P < 0.05, **P < 0.01, and ***P < 0.001, ****P < 0.0001 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31462706), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Insuline-like growth factor (IGF1) antagonized the effects of miR-106a-5p on myogenic differentiation in C2C12. All data were collected from C2C12 myotubes 5 d post differentiation. (A) MyHC immuno-staining of cells incubated in differentiation medium with or without 75 μM IGF1 recombinant protein. Scale bars = 200 μm; (B–D) The statistical results of differentiation index, fusion index and the populations of myotubes, respectively; (E) The expression of miR-106a-5p upon IGF1 stimuli; (F) The mRNA levels of MyoD, MyoG, MyHC in myoblasts cultured in differentiation medium containing 75 μM IGF1 recombinant protein or not; (G) Western-blot analysis of myogenic regulatory factors (MyoD, MyoG, MyHC) and key molecules in PI3K-AKT pathway in cells; (H,I) The statistical results of Figure 3G; (J) Immunostaining of MyHC (red) and DAPI (blue). Scale bars = 200 μm; (K–M) The statistical results of differentiation index, fusion index and the populations of myotubes, respectively; (N) The mRNA levels of MyoD, MyoG, MyHC; (O) Western blot analysis for MyoD, MyoG, MyHC and p-AKT/AKT upon IGF1 challenge; (P) Statistical analysis of MyoD, MyoG, MyHC and p-AKT/AKT levels in Figure 3O. Data were presented as mean ± SEM. n = 3 per group. * p < 0.05, ** p < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30004470), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LukAB is a potent activator of Caspase 1.(A) THP1 cells were intoxicated with 50 ng/mL LukAB for 1 hour and cell lysates were analyzed by immunoblot for Caspase 1 cleavage, which indicates activation. (B and C) THP1 cells were incubated with FLICA-1 (660-YVAD-FMK) then intoxicated with culture filtrates (1% v/v) from the indicated S. aureus stains. After 1 hour, cells were washed, fixed and analyzed by flow cytometry. Panel B shows a representative flow plot from one experiment, and panel C shows the corresponding mean florescence intensities (MFI). (D) THP1 cells were incubated with FLICA-1, intoxicated with purified LukAB (50 ng/mL) for 1 hour, then washed, fixed and analyzed by flow cytometry. (E) FLICA-1 was added to THP1 cells then LukAB (50 ng/mL) was added for time-course samples in descending order. All samples were washed and fixed at the same time, corresponding to different LukAB incubation times, then analyzed by flow cytometry. THP1 cells (F) and primary CD14+ human monocytes (G) were incubated with FLICA-1 and intoxicated with a dose titration of the indicated purified S. aureus leukotoxins for 1 hour. Cells were washed, fixed and analyzed by flow cytometry. Bars represent the standard error of the mean of triplicate samples. EC50 values are also shown. Each graph is representative of three experiments. Primary cell experiments include three independent donors. Asterisks indicate significance at a p-value of ≤ 0.05 by Tukey’s multiple comparisons post-test for 1-way or 2-way ANOVA, as appropriate. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.ppat.1004970), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Glucose fluctuations promoted the activation of NLRP3 inflammasome. (A) Immunofluorescence staining of NLRP3-ASC interaction in rat hearts. The heart sections were labeled with anti-NLRP3 (red), anti-ASC (green), and DAPI (blue) (n = 3 per group). (B–D) The mRNA levels of NLRP3, IL-1 beta and IL-18 in rat hearts of the three groups (n = 4 per group). (E–H) The protein expressions of NLRP3, ASC and cleaved caspase-1 in rat hearts of the three groups (n = 4 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.

EPS15 is targeted via a SPOP/SPOPL binding consensus motif.(A) Cartoon of human EPS15 domain-organization and the amino-acid sequence. Indicated by color code are the SPOP/SPOPL binding site (red) and the lysine residue (yellow), which is ubiquitinated in a CRL3SPOPL–dependent manner in vivo. In addition, the amino-terminal Ca2+-binding EF-hand motifs (EH), the coiled-coil domain involved in dimerization and the two carboxy-terminal ubiquitin-interacting motifs (UIMs) involved in ubiquitin-binding are indicated. (B) EPS15 ubiquitin-profiling. Peptides containing EPS15 modification sites were quantified with LC-MS/MS after enrichment of the K-epsilon -GG motif from whole cell digests of HeLa cells treated with siSPOPL or siControl. Normalized precursor mass intensity profiles for EPS15 sites corresponding to K793, K801 and K693 are shown (raw data in Figure 4—figure supplement 1B). Quantification of the beta -Actin K113 and the polyubiquitin K11 linkage peptide control for comparable enrichment. Data are mean ± SD, N = 3. **p≤0.01. (C) Purified SPOPL was incubated as indicated with GST-tagged wild-type EPS15 or GST-EPS15 mutants, where the predicted SPOPL binding motifs have been mutated individually (GST-EPS15S605-S607A and EPS15S744-S746A, respectively), pulled down with glutathione sepharose (IP [GST]) and bound proteins were analyzed by Coomassie blue staining (upper panel) and immunoblotting (lower panels). Note that SPOPL readily binds to GST-EPS15 and GST-EPS15S605-S607A, but this interaction is strongly reduced with the GST-EPS15S744-S746A mutant. (D) HeLa cells stably expressing GFP-tagged wild-type EPS15, the EPS15S744-S746A or the EPS15K793R mutants from a doxycycline-inducible promoter were transfected as indicated (+) with control siRNA or siRNA depleting SPOPL. The levels of EPS15-GFP, EGFR and for control tubulin (TUB) were analyzed by immunoblotting with specific antibodies. Experiments were quantified in Fiji and the EPS15 levels plotted as fold-increase compared to controls. Data are mean ± SEM, N = 4. *p≤0.05. Note that SPOPL depletion does not further increase the levels of both EPS15 mutants. (E) Total cell extracts were prepared from HeLa cells expressing either GFP-tagged wild-type, the EPS15S744-S746A mutant or the EPS15K793R mutant in the presence (+) or absence (-) of HA-tagged SPOPL overexpression. The levels of EPS15-GFP, SPOPL-HA and control GAPDH were analyzed by immunoblotting. Note that overexpression of SPOPL-HA is able to induce degradation of wild-type but not the EPS15S744-S746A-GFP or the EPS15K793R-GFP mutant.DOI://dx.doi.org/10.7554/eLife.13841.009EPS15 is targeted via a SPOP/SPOPL binding consensus motif.(A) Alignments of the carboxy-terminal domains of EPS15 proteins from various species. Conserved SPOPL-binding motifs and putative ubiquitination sites are highlighted by yellow boxes. (B) Peptides containing EPS15 modification sites were quantified with LC-MS/MS after enrichment of the K-epsilon -GG motif from whole cell HeLa digests treated with siSPOPL and siControl. Raw intensities for each of the triplicate LC-MS/MS runs are shown with each of the siControl conditions scaled to 100% intensity. Normalized precursor mass intensity profiles for EPS15 sites corresponding to K793, K801 and K693 are shown, with only K793 showing significant downregulation in the depletion condition. Quantification of a peptide corresponding to beta -Actin K113 and the poly-ubiquitin K11 linkage peptide is also shown to demonstrate that enrichment variations did not influence the quantification of the EPS15 sites. Additionally, the total ion chromatographic intensities for each run are plotted to provide insight into the consistency of each of the separate experiments performed on different days. Data are mean ± SD, N = 3. (C) HeLa cell lines stably expressing wild-type EPS15-GFP, the EPS15S744-746A-GFP mutant or the EPS15K793R-GFP mutant from the inducible doxycycline-promoter were treated with doxycycline for 3 days, and analyzed by live cell imaging. Displayed are maximal projections of Z-stack acquisitions, fully covering cell height. Scale bar = 10 μm.DOI://dx.doi.org/10.7554/eLife.13841.010 Image collected and cropped by CiteAb from the following open publication (//elifesciences.org/articles/13841), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Examples of PNUTS staining: (a) comparison of PNUTS staining in (1) normal and (2) cancerous prostate glands of the same TMA spot. Cancer spots with (b) lack of staining and (c) weak, (d) moderate, and (e) strong staining. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32377272), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The mRNA and protein expression of cytochrome c oxidase 4 (COX4), toll-like receptor (TLR) 9, myeloid differentiation factor 88 (MyD88), and nuclear factor (NF)-kappa B in lung tissues from spontaneous breathing group (CON group), normal tidal volume (NTV) group, high tidal volume (HTV) group, chloroquine (CQ) pretreatment upon HTV stimulation group (HTV + CQ). (A) Levels of COX4, TLR9, MyD88, and NF-kappa B mRNA. (B) Levels of COX4, TLR9, MyD88, and NF-kappa B protein by Western blot. (C) Relative expression of COX4, TLR9, 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. NTV group; and CP < 0.05 vs. HTV 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.

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.

Quantification of knockdown of beta 1 integrin in hS/PC microstructures. hS/PC microstructures formed in HA-based hydrogels and were transfected with scrambled siRNA or ITGB1 siRNA. Immunocytochemistry was used to determine beta 1 integrin expression and spatial distribution of beta 1 integrin 46 h post-transfection. Image analysis software was used to quantify beta 1 integrin expression at microstructure surfaces from confocal micrographs and coverage indices were calculated for scrambled siRNA (A) and ITGB1 siRNA (B) groups where a 63% reduction in beta 1 integrin expression at microstructure surfaces was quantified (C). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31750298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Rb

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	NB600-408AF350
Alexa Fluor 405	NB600-408AF405
Alexa Fluor 488	NB600-408AF488
Alexa Fluor 532	NB600-408AF532
Alexa Fluor 594	NB600-408AF594
Alexa Fluor 647	NB600-408AF647
Alexa Fluor 700	NB600-408AF700
Alexa Fluor 750	NB600-408AF750
Allophycocyanin	NB600-408APC
Biotin	NB600-408B
DyLight 350	NB600-408UV
DyLight 405	NB600-408V
DyLight 488	NB600-408G
DyLight 550	NB600-408R
DyLight 594	NB600-408DL594
DyLight 650	NB600-408C
DyLight 680	NB600-408FR
DyLight 755	NB600-408IR
FITC	NB600-408F
HRP	NB600-408H
Janelia Fluor 549	NB600-408JF549
Janelia Fluor 646	NB600-408JF646
PE	NB600-408PE
PerCP	NB600-408PCP

compare

(select up to 3 products from this page to compare)

BC100-494

PINK1 Antibody - BSA Free

(13 Reviews)

(247 Publications)

0.1 ml

BC100-494

$PINK1/Parkin-mediated mitophagy. Western Blot of mitochondrial and cytosolic fractions for PINK1, Parkin, and ubiquitin. E Quantitation of protein levels, normalized to VDAC and GAPDH, Ubiquitin: n = 6, PINK1: n = 5, Parkin: n = 8. R, post-reoxygenation. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33980811/) licensed under a CC-BY license.$

Confocal microscopy analysis of the mitophagy initiation in the RPE cells by staining PINK1 and PARKIN. One-year-old WT and dKO mice focusing on the RPE cells in the vicinity of the optic nerve (a,e). PINK1 (b, red) and PARKIN (c, green) were double-stained and the merged image (d) was used to count the colocalized puncta from WT. Similarly, in dKO PINK1 (f, red) and PARKIN (g, green) were double-stained, and the merged image (h) was used to count the colocalized puncta. dKO = NFE2L2/PGC1a double knockout. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183173/) licensed under a CC-BY license.

Western blot image of PINK1 antibody (BC100-494) in multiple cells lines. Human HeLa (lane 1), Mouse NIH-3T3 (lane 2), L929 (lane 3) and Rat PC12 (lane 4) whole cell protein were separated by SDS-PAGE on a 7.5% polyacrylamide gel. Protein was transferred to PVDF membrane and probed with 2 ug/mL BC100-494 in 1% BSA and detected with an HRP-conjugated anti-rabbit secondary antibody using chemiluminescence. Observed molecular weight ~55 kDa (arrowhead).

Analysis of PINK1 in mouse liver and hypatocytes using PINK1 antibody. Observed molecular weight ~55 kDa. WB image submitted by a verified customer review.

Pathogenic mutants of Parkin are subjected to Ser65 phosphorylation. Phos-tag Western blotting for Parkin and Western blotting for PINK1 were performed using Parkin WT and a series of pathogenic mutants. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep01002) licensed under a CC-BY license.

Alteration of mitochondria and PD associated proteins in SH-SY5Y cells with telomere removal by CRISPR-Cas9. Representative Western blot of PGC-1alpha, NRF1, and PINK1 in SH-SY5Y cells transfected with either gTel or gCont (72 h). Beta-actin served as a loading control. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/18/10/2093), licensed under a CC-BY license.

35 ug Neuro2A whole cell lysate separated on 8% PAGE and stained for PINK1 (1:1000 in 5% milk powder in TBST; secondary antibody AP at 1:5000). WB image submitted by a verified customer review.

Rabbit heart tissue. IHC-P image submitted by a verified customer review.

HEK293 cells were co-transfected with PINK1 siRNA (#1 or #2) or scrambled siRNA (scrambled) and untagged wild-type (WT) or Ser65Ala (S65A) mutant Parkin as indicated using TransFectin reagent (Bio-Rad). 48 hrs post-transfection, cells were treated with/without 10 uM CCCP for 3 h. 0.25 mg of 1% Triton whole-cell lysate were subjected to immunoprecipitation with GST-Parkin antibody (S966C) covalently coupled to protein G Sepharose and then immunoblotted with anti-phospho-Ser65 antibody in the presence of dephosphorylated peptide. 5% of the IP was immunoblotted with total anti-Parkin antibody. 0.25 mg of whole-cell lysates were immunoprecipitated with anti-PINK1 antibody (S085D) and immunoblotted with anti-PINK1 antibody. Representative of three independent experiments. Image collected and cropped by CiteAb from the following publication (//rsob.royalsocietypublishing.org/cgi/doi/10.1098/rsob.120080) licensed under a CC-BY license.

Characterisation of mitochondrial content and function in PINK1-/- platelets. Cropped immunoblots showing PINK1 expression in 10 uM CCCP (6 hours) treated WT, but not KO platelets by IP (upper panel) with loading control of IP inputs by blotting for PINK1 (lower panel). Uncropped blots for PINK1 are provided in Supplementary Fig. S1b. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-32716-4), licensed under a CC-BY license.

Representative TEM picture. The red and green arrows indicate PINK and PARKIN immunogold particles in the dKO RPE samples, respectively (e). ML, melanosome. Scale = 0.2 um. Mitochondria (M). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183173) licensed under a CC-BY license.

Protein content and oxidation. Gastrocnemius muscle was analyzed by immunoblotting (A) for oxidatively modified protein, STIM1, PARKIN, PINK1, PGC‐1 alpha , VDAC1, and 4HNE (B). Data are means ± SEM. *Significantly different from Tp53inp1+/+.

USP30 restricts basal pexophagy. H). Quantification of Keima-SKL

$The FANCD2 NLS is required for efficient FANCD2 and FANCI monoubiquitination and chromatin association.(A) FA-D2 cells stably expressing LacZ, FANCD2-WT, FANCD2-K561R, FANCD2-∆N57, FANCD2-∆N100 and FANCD2-3N were incubated in the absence and presence of 250 nM MMC for 18 h, and whole-cell lysates were immunoblotted with antibodies to FANCD2, V5, FANCI and alpha -tubulin. The FANCD2 and FANCI L/S ratios are the ratios of monoubiquitinated to nonubiquitinated protein, and were calculated by measuring protein band intensities using ImageJ image processing and analysis software (//rsb.info.nih.gov/ij/). (B and C) FA-D2 cells stably expressing FANCD2-WT, FANCD2-∆N57, FANCD2-∆N100 and FANCD2-3N were treated as above and cell pellets were fractionated into soluble (S) and chromatin-associated (C) fractions. Fractions were immunoblotted with antibodies against V5, FANCI, alpha -tubulin and H2A. W, unfractionated whole cell extract. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24278431), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Immunoblot analyses of protein expression for Nrf2 and antioxidant enzymes.A. Analysis of nuclear Nrf2 in young and old mice subjected to EES. In sedentary mice, Nrf2 protein levels were decreased significantly in young versus old mice. EES exacerbated the decrease of nuclear Nrf2 in old mice. Blots/values represent n = 4–6 from each group. *p10 embryos/sample). The blots were probed with antibodies against Lc3 and Actin as a loading control. Western blots were repeated at least three times with independent extracts. (C) Quantification of Lc3-II fold changes in WT and mutant embryos in absence or presence of Baf A1. Western blot band intensities were quantified by Lab Image. Data is combined from three independent experiments. (D) Representative confocal micrographs of GFP-Lc3 puncta present in the tail fin of optn+/+, optn delta 5n/ delta 5n, p62+/+ and p62 delta 37n/ delta 37n at 4 dpf. Scale bars, 10 μm. (E). Quantification of the number of GFP-Lc3 puncta in optn+/+, optn delta 5n/ delta 5n, p62+/+ and p62 delta 37n/ delta 37n larvae with and without Baf A1 treatment. Each larva was imaged at a pre-defined region of the tail fin (as indicated by the red boxed area in Fig3 A) (≥11 larvae/group). Results are accumulated from two independent experiments. ns, non-significant, *p 12 months) were injected i.v. with siScr or siMST. Twenty‐four hours after siRNA injection, a 70% PH was performed and remnant/regenerating liver tissue was harvested 40 h later. p.i. of the livers was calculated by IHC staining of Ki67‐positive hepatocytes and livers were classified as (−) non‐regenerating or (+) regenerating based on the percentage of positive cells. Non‐surviving animals were sacrificed before the 40‐h end time point. “n” indicates the number of animals per group.Ki67 immunostaining of the regenerating aged mice livers, 40 h post‐PH. Sections were scanned using 3DHistech Pannoramic MIDI Scanner and quantitated with Quant Center 2.0 software. p.i. values are provided on the image.Representative photomicrograph of an aged liver treated with siMST and stained with H&E and by IHC for CK19 and Ki67. Arrows indicate ductal regions with no signs of reaction or oval cell expansion.Quantitative RT–PCR analysis of RNA isolated from mouse liver for Foxm1B, Birc5 and Ccnb1 at 0 and 40 h post‐PH. Log2 fold change was calculated using non‐transfected/non‐resected mouse liver as a control. Representative results from a single experiment with n = 6 animals per group are shown. Paired, two‐tailed Student's t‐test was used to calculate the significant change in signals between liver tissues at the time of resection (0 h) compared to 40 h post‐PH.Percentage of Ki67‐positive hepatocytes in aged and aged + siMST 40 h post‐resection. Representative results from a single experiment with n = 6 independent aged animals for group are shown. Two‐tailed Student's t‐test was used to calculate the significance of percentage of positive hepatocytes of siMST‐treated animals compared to non‐treated controls.Endpoint liver weight was taken of the remnant lobe and expressed as a percentage to total body weight. Representative results from a single experiment with n = 6 independent animals for group expect for control group where n = 6 are shown. Estimated liver‐to‐body weight ratio before PH in mice = 3.85 ± 0.05 (SD). Unpaired, two‐tailed Student's t‐test was used to calculate the significance of each aged group in comparison with the control young group.Hepatocyte geometric diameter was determined (see Materials and Methods). Representative results from a single experiment with n = 3 independent animals per group. Unpaired, two‐tailed Student's t‐test was used to calculate the significant change in hepatocyte size in liver tissue with and without siMST 40 h post‐PH.Data information: Bars represent mean ± SD. Scale bars, 50 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27940445), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Rb

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	BC100-494AF350
Alexa Fluor 405	BC100-494AF405
Alexa Fluor 488	BC100-494AF488
Alexa Fluor 532	BC100-494AF532
Alexa Fluor 594	BC100-494AF594
Alexa Fluor 647	BC100-494AF647
Alexa Fluor 700	BC100-494AF700
Alexa Fluor 750	BC100-494AF750
Allophycocyanin	BC100-494APC
Biotin	BC100-494B
DyLight 350	BC100-494UV
DyLight 405	BC100-494V
DyLight 488	BC100-494G
DyLight 550	BC100-494R
DyLight 594	BC100-494DL594
DyLight 650	BC100-494C
DyLight 680	BC100-494FR
DyLight 755	BC100-494IR
FITC	BC100-494F
HRP	BC100-494H
Janelia Fluor 549	BC100-494JF549
Janelia Fluor 646	BC100-494JF646
PE	BC100-494PE
PerCP	BC100-494PCP
mFluor Violet 450 SE	BC100-494MFV450
mFluor Violet 500 SE	BC100-494MFV500
mFluor Violet 610 SE	BC100-494MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	BC100-494SS

compare

(select up to 3 products from this page to compare)

NB100-143

Nbs1 Antibody

(8 Reviews)

(199 Publications)

0.05 ml

NB100-143

Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - ICC/IF analysis of Nbs1 in HeLa cells with Nbs1 Antibody [NB100-143]. Image from verified customer review.

Immunohistochemistry-Paraffin: Nbs1 Antibody [NB100-143] - FFPE human testis using Nbs1 antibody [NB100-143] at 1:200 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10 mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Staining was performed by Histowiz.

Western Blot: Nbs1 Antibody [NB100-143] - Analysis of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal NBS1 antibody [NB100-143]. Observed Molecular Weight at ~95 kDa.

<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Detection of NBS1 in Human Bone Osteosarcoma Epithelial Cells (U2OS whole cell lysate) using Nbs1 Antibody [NB100-143] at a dilution of 1:1000. Specificity was confirmed using a siRNA anti-NBS1 (targeting sequence: GGAAGAAACGUGAACUCAA). Image provided by Sebastien Britton of the Institute of Pharmacology and Structural Biology.

Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.

Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - Staining of HeLa cells using Nbs1 Antibody [NB100-143].

<b>Genetic Strategies Validation. </b>Knockdown Validated: Nbs1 Antibody [NB100-143] - TOPBP1 recruitment in response to rDNA breaks. TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1-delta-N cells and NBS1-delta-N cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317/) licensed under a CC-BY license.

HPV16 E2 partially colocalizes with the MRN complex proteins Mre11 and Nbs1. C33a cells were transfected with an HPV16 E2 expression plasmid, fixed in ice-cold methanol, and stained with an E2-specific antibody (green). DNA was stained with Hoechst 33342 (blue). (A) Endogenous Nbs1 was detected with an Nbs1-specific antibody (red/gray). (B) Endogenous Mre11 was detected with an Mre11-specific rabbit antibody (red/gray). Bar, 5 μm. Digital zoom is shown at the bottom.

TOPBP1 recruitment in response to rDNA breaks. b) TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1deltaN cells and NBS1deltaN cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317), licensed under a CC-BY licence.

ATM promotes cell migration and invasion independently of DNA DSB signaling in MDA-MB-231 cells.(B and C) Quantification of wound healing (B) and siRNA depletions (C) in (A). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26030852), licensed under a CC-BY licence.

KSHV LANA recruits MRN (Mre11-Rad50-NBS1) complex.(A) Co-immunoprecipitation of endogenous LANA and MRN proteins in BC3 cells. Cells were lysed using TBS-T buffer and the cell lysate was incubated with benzonase. After centrifugation, supernatant was incubated overnight with anti-LANA or IgG-control beads. The precipitated complexes were analyzed for the presence of endogenous Rad50, Mre11 and NBS1 by SDS-PAGE and immunoblotting. For the input, see Materials and methods. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006335), licensed under a CC-BY licence.

Replication centers of the integrated HPV recruit Mre11-Nbs1-Rad50 complex and Ku70/80 heterodimer.HeLa cells were transfected and analyzed as described previously. Co-immunostaining of HPV18 E1 (Alexa Fluor 568, second column) and the following proteins are presented: Mre11, Nbs1, Rad50, and Ku70/80 proteins (Alexa Fluor 488, first column). The localizations of the E1 and the respective DNA repair proteins are also shown in the third column as a merged image and DAPI stained nuclei are presented in the fourth column. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19390600), licensed under a CC-BY licence.

TRIB3 suppresses the functions of the UBE3B:MYC axis to attenuate lymphomagenesis.a Occupancy heatmap of genome-wide MYC peaks in MYCWT and MYCK427R Raji cells in a window of ±10 kb surrounding the transcription start site (TSS). b Distribution of MYC tags in MYCWT and MYCK427A Raji cells. Binding is shown for a window of ±2 kb around MYC tags as reference coordinates. c GSEA shows global downregulation of MYC target genes in Ad-UBE3B versus Ad-CTRL Raji cells. d Metagene plots of global RNAPII occupancy at gene bodies in Raji cells with or without UBE3B overexpression. e Colony-forming capacity of Raji cells with or without UBE3B overexpression. The data are presented as the means ± S.E.M from three independent experiments. Statistical significance was determined by two-tailed Student’s t test. P value: 0.00047. f Relative cell viabilities of Raji cells with overexpression of the indicated genes for the indicated times. The colors represent different time points; the diameter indicates the relative cell viability. The data are presented as the means ± S.E.M from three independent experiments. g Schematic strategy for studying BCL development in MycEμ mice with the indicated infection of Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3 in vivo. h Data are the spleen weights of MycEμ mice (n = 8 per group) with overexpression of the indicated genes. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 2.077 × 10−5, 0.0009. i Data are representative LNs in MycEμ mice overexpressing Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3. Scale bar, 0.5 cm. j Cell proliferation was determined by Ki67 staining in the spleens of the indicated mice (n = 6 per group). Data are representative images of Ki67 staining and statistical analyses of Ki67-positive cells. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 1.352 × 10−12, 3.674 × 10−8. Scale bar, 50 μm. k Approaches to defining the self-renewal ability of mouse LCs from the indicated mice (5 months old). l Colony-forming ability of BCL cells isolated from MycEμ mice (n = 6 per group) overexpressing Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 4.318 × 10−5, 0.0001. m The tumorigenicity of BCL cells from the indicated mice was compared by limiting dilution transplantation into NSG mice; n = 8 mice per group. n Schematic strategy for studying BCL development in MycEμCD19CreTrib3F/+ mice infected with or without lentivirus Ube3bCas9. o Kaplan–Meier survival curves for MycEμCD19CreTrib3F/+ mice infected with or without lentivirus Ube3bCas9 (n = 8 per group). Statistical difference was determined by two-sided log-rank test. P value: 0.0002. p Expression of MYC in the spleens of MycEμCD19CreTrib3F/+ mice (5 months old) infected with or without lentivirus Ube3bCas9. The data are presented as presentative from three independent experiments. q Colony-forming ability of BCL cells isolated from the LNs of the indicated mice (n = 6 per group). The data are representative or the means ± SEM of three assays. Statistical significance was determined by two-tailed Student’s t test. P value: 5.417 × 10−5, 0.0042. The MycEμCreCD19Trib3F/+ mice are heterozygous for the MycEμ allele. 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/33298911), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$The BNIP3 C-terminus can be phosphorylated.(A) Western blot detection of immunoprecipitated BNIP3 using an alpha -PKA substrate antibody specific to the phosphorylated RRXS/T sequence, located at the BNIP3 C-terminus and adjacent to the transmembrane (TM) domain. Results shown for 4 cell types: (left to right) HEK 293 cells expressing exogenous BNIP3 (dimer, 60 kD), and A549, MDA-MD-231, and AU565 cells expressing endogenous BNIP3 (monomer, 30kD). Lane 1 of each Western blot contains the whole cell lysate (WCL). (B) LC-MS/MS analysis of BNIP3 phosphorylation in HEK 293 cells with normal or elevated cAMP (8-Bromo-cAMP), showing peptide coverage (gray) and phosphorylation sites (red). The TM domain is underlined. (C) Table of BNIP3 phosphopeptides identified by LC-MS/MS, showing the percent probability, ion charge, actual and observed masses, and mass error (Da and ppm) for each peptide. Peptides shown are from analysis of BNIP3 purified from HEK 293 cells with elevated cAMP levels. (D) Schematic of the BNIP3 protein sequence, showing each C-terminal mutation representing phosphomimetic or nonphosphorylated BNIP3. (E) Expression of BNIP3 phosphomutants from stable doxycycline-inducible HEK 293 Tet On cells, treated with doxycycline (Dox) for 48 hr. (F) Subcellular localization of BNIP3 phosphomutants, showing Western blot of cytosolic and mitochondrial fractions. (G) Alkaline extraction of mitochondria-associated proteins, showing alkaline extract of the mitochondrial pellet and the alkaline-resistant mitochondrial pellet from cells expressing each BNIP3 phosphomutant. All blots are representative of at least 3 independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26102349), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$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.$

mTOR complex protein expressions and rictor phosphorylation at Ser1235.Cardiomyocytes were pretreated for 30 min with 20 nM rapamycin and then stimulated with 10 nM IGF-1 in presence or absence of 10 nM E2 for 24 h. A, shown are representative western blots for mTOR, rictor and raptor and B,C,D, quantitative analysis with mean ± SEM of fold stimulation by IGF-1 of at least 3 independently performed experiments (B,C,D). * p < 0.05, **p < 0.0095. Exposure to rapamycin lead to downregulation of mTOR and rictor, which were more pronounced under culture conditions without E2. E, Western blots for GSK3 beta -pS9, GSK3 beta , rictor pS1235 and rictor and F,G,H,I quantitative analysis of at least 3 independently performed experiments indicate that rictor phosphorylation at S1235 by GSK-3 beta which has been reported to interfere with Akt-substrate binding to mTORC2, thereby downregulating mTORC2 activity. IGF-1 induced strong phosphorylation of GSK-3 beta at Ser9 in the absence and presence of E2, however, rapamycin pretreatment only reduced this increased phosphorylation in E2 co-treated cardiomyocytes, indicating increased activity of GSK-3 beta . This higher activity was not associated with increased phosphorylation of rictor at S1235. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0123385), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ha, Ma, Pm

Species Glossary

Reactivity: Hu, Mu, Ha, Ma, Pm

Applications:

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

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

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

compare

(select up to 3 products from this page to compare)

NB400-135

CHREBP Antibody - BSA Free

(7 Reviews)

(145 Publications)

0.1 ml

NB400-135

Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Staining of human colon, epithelium at a 40X magnification.

Chromatin Immunoprecipitation: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Effects of glucose on ChREBP binding.HepG2 cells were treated with low (2.7 mM) and high (25 mM) glucose for 8 h. Chromatin was isolated and fragmented, and ChIP was performed with control IgG or anti-ChREBP antibody. Validated primers for each gene were used for quantitative real-time PCR. The data presented as fold increase for the signal from anti-ChREBP relative to control IgG. The negative control, Cyclo, showed no enrichment (data not shown). Values represent the mean +/- S.D. of three independent samples. *p<0.005 vs. IgG, #p<0.0001 vs. 2.7 mM glucose with anti-ChREBP. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0022544), licensed under a CC-BY license.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in 20 ug of human hepatocyte lysate using NB400-135. 5-10 second film exposure.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in liver nuclear extracts from well-fed rats. 7% SDS-PAGE gel, 1:1000 dilution of NB400-135. Photo courtesy of Dr. Uyeda, UT Southwestern University.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - RetSat depletion in mouse liver reduces protein levels and target gene expression of ChREBP. RetSat and ChREBP protein expression by immunoblotting. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Protein expression levels of carbohydrate-responsive element-binding protein (ChREBP), in livers of rats receiving normal water (CON), a 13% (w/v) glucose solution (GLU), a 13% (w/v) fructose solution (FRUC), or a 0.4% (w/v) aspartame solution (n = 6 per diet group). All data were normalized to beta-actin expression levels and are expressed relative to the controls (CON). Data are expressed as means +/- SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. CON; +p < 0.05, ++p < 0.01, +++p < 0.001 vs. ASP; p < 0.01, p < 0.001 vs. GLU. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/5/476), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - HeLa cells were fixed for 10 minutes using 10% formalin and permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-ChREBP (NB400-135) at a 1:200 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-stained at 1:1000 and detected with an anti-mouse DyLight 550 (Red) at a 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunohistochemistry: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Analysis of CHREBP in mouse liver using DAB with hematoxylin counterstain.

<b>Genetic Strategies Validation. </b>Knockout Validated: CHREBP Antibody - BSA Free [NB400-135] - Immunoblot analysis of ChREBP in liver lysates of control and L-Chrebp -/- mice. Aliquots (60 ug of protein) of liver whole-cell lysates were subjected to SDS-PAGE and immunoblot analysis with anti-ChREBP and anti-calnexin antibodies. ChREBP delta denotes a truncated aberrant ChREBP protein present only in lysates prepared from L-Chrebp -/- livers. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29335275/) licensed under a CC-BY license.

Analysis of protein levels in livers transfected with GK and GKA456V. Livers excised from mice in postabsorptive state were homogenized and resolved by Western blot. (a, b) Representative blots from three independent experiments. The densitometric analysis is presented (N = 4, *P < 0.05 versus pControl, ***P < 0.001 versus pGKA456V). (c) Liver sections of 5-hour fasted mice injected with pControl, pGK, or pGKA456V were immunostained with Glc6Pase antibody. TO-PRO-3 was used to visualize nuclei.

LXR mediate the induction of lipogenesis induced by an oleic acid-rich diet. (E) Cytoplasmic and nuclear expression levels of LXR, SREBP-1c and ChREBP assayed by Western Blotting. Data are the mean+/-SEM of values measured in LXR+/+ and LXR-/- mice fed REF or OLIV diet. a Significant genotype effect. b Significant difference versus REF diet (n = 6 mice per group). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28732092), licensed under a CC-BY licence.

ChREBP knockdown inhibited glycolysis, lipogenesis and p21 in HT29 cells. (B) Western-blot of ChREBP, phospho-p53 and p21 and their quantification on the right. beta-actin was served as a loading control. Proteins were extracted from cells transfected with sicontrol and siChREBP after 48 hours. The quantification of western blot was normalized to beta-actin. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32144313), licensed under a CC-BY licence.

Effects of glucose on ChREBP binding.HepG2 cells were treated with low (2.7 mM) and high (25 mM) glucose for 8 h. Chromatin was isolated and fragmented, and ChIP was performed with control IgG or anti-ChREBP antibody. Validated primers for each gene were used for quantitative real-time PCR. The data presented as fold increase for the signal from anti-ChREBP relative to control IgG. The negative control, Cyclo, showed no enrichment (data not shown). Values represent the mean +/- S.D. of three independent samples. *p<0.005 vs. IgG, #p<0.0001 vs. 2.7 mM glucose with anti-ChREBP. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21811631), licensed under a CC-BY licence.

Sucrose intake increases hepatic triglyceride content via sex-specific mechanisms. e) Representative western blots demonstrating that the abundance of proteins encoded by the transcripts differentially expressed (as well as ChREBP and its target PKLR) between males and female mice in response to sucrose intake. Statistics were derived following densitometric quantification of bands from samples run on a single gel that were normalized to total protein and then log transformed and compared using two-way ANOVA with post hoc Tukey's tests (FAS: ap= 1.43-4, bp = 1.55-4, dp = 0.044, ep = 2.80-6; pACC: ap = 0.001, bp = 0.007, ep = 2.8-4, fp = 0.041; ACC: ap = 0.001, bp = 0.003, ep = 2.99-4, fp = 0.014; ChREBP: ep = 0.024, fp = 0.010; MC: n = 6, MS: n = 6, FC: n = 6, FS: n = 6). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/36229459), licensed under a CC-BY licence.

FXR inhibits glucose-induced proglucagon expression. (c) ChREBP and FXR western-blots after FXR immunoprecipitation on lysates from cytoplasm and nucleus of GLUTag cells treated or not with GW4064 (5 umol L-1) in presence or not of glucose (5.6 mmol L-1) (performed 2 times). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms8629), licensed under a CC-BY licence.

Raffinose stimulates transcription of genes involved in epidermal barrier function in HaCaT cells.(a and b) HaCaT cells were treated with vehicle, 1 uM or 10 uM raffinose (Raf), or 1 uM TO901317 (T17) for 24 h. Expressions of transcripts (a) and proteins (b) were analyzed by qRT-PCR or western blotting, respectively. FLG; filaggrin. IVL; involucrin, LOR; loricrin, AQP3; aquaporin3. (c) HaCaT cells were transfected with siGFP control, siLXRalpha, or siLXRbeta, and then treated with 1 uM raffinose for 24 h. Expression of proteins was analyzed by western blotting. The original blots are shown in Supplementary Fig. S9. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28266648), licensed under a CC-BY licence.

Hepatic expression of mRNAs encoding carbohydrate response element-binding protein (ChREBP) (a), liver pyruvate kinase (LPK) (c), and microsomal triglyceride transfer protein (MTTP) (d), and nuclear ChREBP protein (b) in water-control, 10% fructose solution-control, and fructose pair-fed oleanolic acid- (OA-) treated rats at week 10. Animals were administered with OA (25 mg/kg/day) or vehicle (OA: 0 mg/kg, 5% Gum Arabic) by oral gavage daily for 10 weeks. mRNA was determined by real-time PCR. Protein expression was determined by Western blot. Data are means +/- SEM (n = 6 each group). *P < 0.05. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23737835), licensed under a CC-BY licence.

Protein expression levels of (D) carbohydrate-responsive element-binding protein (ChREBP); (E) 128 kDa precursor sterol regulatory element-binding protein-1c (SREBP-1c); and (F) 65 kDa cleaved SREBP-1c, in livers of rats receiving normal water (CON), a 13% (w/v) glucose solution (GLU), a 13% (w/v) fructose solution (FRUC), or a 0.4% (w/v) aspartame solution (n = 6 per diet group). All data were normalized to beta-actin expression levels and are expressed relative to the controls (CON). Data are expressed as means +/- SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. CON; +p < 0.05, ++p < 0.01, +++p < 0.001 vs. ASP; **p < 0.01, ***p < 0.001 vs. GLU. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/5/476), licensed under a CC-BY licence.

Optical redox ratio (ORR) demonstrates reduced glycolytic phenotype following 24 hours of YC-1 treatment. ORR of A549 and A549RR cells before, 12 and 24 hours following 50 μM YC-1 treatment to inhibit HIF-1 (a,b). Immunoblotting for HIF-1 alpha (c) and PDK-1 (d) before and 24 hours following YC-1 treatment to verify in of HIF-1 alpha . Representative immunoblots were horizontally cropped at the molecular weight indicated (e). Uncropped exposures can be seen in Supplemental Fig. 1. Experiments were performed in triplicate across 3 independent experiments. *p < 0.05 compared to A549 0 hr control, †p < 0.05 compared to A549RR 0hrs. Scale bar in images represents 50 μm. ME – Main effect of cell type and time; however, no significant interactions were found between the two main effects. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41598-018-27262-y), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Excessive AP-endonuclease activity in cells with p53 impairment leads to accumulation of genomic instability. (A) Representative western blotting analysis on WI38 (SV40) cells shows rescue of gamma H2AX staining upon co-depletion of XRCC1 and APE1. (B) Neutral Comet assay on WI38 (SV40) fibroblasts shows accumulation of DSBs upon XRCC1-depletion and rescue after co-depletion of XRCC1 and APE1. Results are expressed as mean ± SD of three independent experiments. (C) Representative western blotting analysis on WI38 (SV40) cells shows rescue of gamma H2AX staining after depletion of XRCC1 in presence of APE1 inhibitor III (APE1i III, 5 μM for 24 h), or AR03 (2.5 μM for 24 h). Actin was used as loading control in all western blotting experiments. Image collected and cropped by CiteAb from the following open publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw015), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effects of resveratrol on the expression of SIRT1, PGC-1 alpha , HIF-1 alpha and apoptosis proteins in vitro. (A) The expression of SIRT1, PGC-1 alpha , and Bcl-2 proteins were lower in iohexol treated HK-2 cells compared with control cells, which was reversed by treatment with resveratrol. The expression of HIF-1 alpha , Bax, cleaved caspase-3, and Cyt-C were markedly increased after iohexol injection, which was reversed by treatment with resveratrol. Furthermore, this effect was enhanced by HIF-1 alpha inhibitor, 2-MeOE2. (B–H) Relative densitometry of SIRT1–PGC-1 alpha –HIF-1 alpha signaling proteins expressed as mean ± standard error. *P < 0.05 vs. Cont; #P < 0.05 vs. PC–AKI. Cont, control; Res, resveratrol; PC–AKI, post-contrast acute kidney injury; SIRT1, silent information regulator l; HIF-1 alpha , hypoxia-inducible transcription factor-1 alpha ; Cyt-C, cytochrome C; PGC-1 alpha , peroxisome proliferator-activated receptor gamma coactivator-1 alpha; Ex527, SIRT1 specific inhibitor; LG, low glucose. Groups: Res, HG+res+iohexol; Ex527, HG+Ex527+iohexol; PC–AKI, HG+iohexol; 2-MeOE2, HG+res+2-MeOE2+iohexol; Cont, LG. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31402864), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

EpEX and EpCAM activate a STAT3-HIF2 alpha signal for EpEX/EpCAM-mediated iPSC formation.(A) iPSCs were infected with two different EpCAM shRNAs (two clones, #1 and #2). The protein expressions of EpCAM and HIF2 alpha were detected by Western blotting. (B) MEFs were stimulated by EpEX (1 μg/mL) at the indicated times. Nuclear-translocation was detected with a specific antibody against HIF2 alpha (n = 3). (C) Immunofluorescence staining was performed to detect subcellular localization of HIF2 alpha . Nuclei were stained with DAPI. Scale bar: 10 μm. (D) MEFs were treated with STAT3 inhibitor (WP1066, 10 μM), and then stimulated with EpEX for 30 min. The nuclear-translocation of HIF2 alpha was detected by Western blotting with anti-HIF2 alpha antibody (n = 3). (E) iPSC morphology was observed at day 20 after induction. Reprogramming of Oct4-GFP MEFs was induced by transfection of OSKM, OE + EpEX, and KE + EpEX with or without STAT3 inhibitor WP1066, or HIF2 alpha shRNA (n = 3). Scale bar: 50 μm. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep41852), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Cell cycle block under PHD3 depletion is accompanied by p27 induction. a PHD3 depletion induces a cell cycle block in G0/G1. HeLa and renal cell adenocarcinoma cells (786-O) were transfected with control (siScr) or PHD3 targeted (siPHD3) siRNA followed by synchronization at G0 and 24-h hypoxic exposure. Cell cycle progression was monitored by FACS analysis 8 h after cell cycle release. The combined means of three independent experiments are presented (±SEM) shown in the tables below. b PHD3 depletion induces p27 expression in HeLa cells and in 786-O cells under hypoxia (1 % O2) and normoxia (21 % O2) by siPHD3 and independent adenoviral shRNA against PHD3. p21 or p16 expression is not elevated by PHD3 knockdown. c Depletion of either PHD1 or PHD2 by siRNA does not increase p27 expression in 786-O cells Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GAD65/67-positive neurons expressed HIF-1 alpha under hypoxic conditions. A) HIF-1 alpha expression co-localized with GAD65/67-ir in neurons exposed to hypoxia when compared to normoxia (upper panel) or GAD65/67-negative neurons in hypoxia (bottom panel, open arrow). B) Quantification shows the percentage of HIF-1 alpha -expressing GAD65/67-positive neurons after hypoxia in vitro (mean ± SD; from n = 6 cultures). C)In vivo immunostaining illustrates HIF-1 alpha -positive (bottom panel, solid arrow) and HIF-1 alpha -negative (bottom panel, open arrow) in GAD65/67-ir neurons in the ipsilateral region, whereas the contralateral region shows no HIF-1 alpha staining in GAD65/67-ir neurons (see Figure 1 for region selection). Scale bars, 10 μm (A); 20 μm (B). Image collected and cropped by CiteAb from the following open publication (//actaneurocomms.biomedcentral.com/articles/10.1186/2051-5960-2-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Absence of Zizimin proteins, but normal numbers of hematopoietic cells in KO mice. (A-B) Western blotting for Ziz2 (A) or Ziz3 (B) Protein lysates (30 μg/lane) were loaded and designated antibodies were reacted with the membranes. Replicated membranes were used for all antibodies. Zizimin proteins were absent in KO mice (8 weeks old, male). (C-F) The numbers of hematopoietic cells were counted after the hemolytic reaction (C-E) or flow cytometric analysis (F). No significant difference was observed among the groups (C-F). Three mice (8 weeks old, female) per group from three independent experiments (one mouse per group per experiment) were used. 2KO: Ziz2 KO. 3KO: Ziz3 KO. Image collected and cropped by CiteAb from the following open publication (//immunityageing.biomedcentral.com/articles/10.1186/s12979-015-0028-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemical analysis of CNHCs with antibodies against the RCC marker CAIX. Clusters of CNHCs cytomorphologically classified as uncertain malignant (−UMF) with cytoplasmic positive staining with antibodies against the RCC marker CAIX (A). Clusters of CNHC-UMF and -BF without reactivity for CAIX antibodies (B and C, respectively). A single CNHC-MF with positive cytoplasmic (D) and without staining for CAIX (E). Single CAIX-negative CNHC-UMF and -BF (F and G, respectively). Image collected and cropped by CiteAb from the following open publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-214), 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:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-135AF350
Alexa Fluor 405	NB400-135AF405
Alexa Fluor 488	NB400-135AF488
Alexa Fluor 532	NB400-135AF532
Alexa Fluor 594	NB400-135AF594
Alexa Fluor 647	NB400-135AF647
Alexa Fluor 700	NB400-135AF700
Alexa Fluor 750	NB400-135AF750
Allophycocyanin	NB400-135APC
Biotin	NB400-135B
DyLight 350	NB400-135UV
DyLight 405	NB400-135V
DyLight 488	NB400-135G
DyLight 550	NB400-135R
DyLight 594	NB400-135DL594
DyLight 650	NB400-135C
DyLight 680	NB400-135FR
DyLight 755	NB400-135IR
FITC	NB400-135F
HRP	NB400-135H
Janelia Fluor 549	NB400-135JF549
Janelia Fluor 646	NB400-135JF646
PE	NB400-135PE
PerCP	NB400-135PCP
mFluor Violet 450 SE	NB400-135MFV450
mFluor Violet 500 SE	NB400-135MFV500
mFluor Violet 610 SE	NB400-135MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-135SS

compare

(select up to 3 products from this page to compare)

NB100-56566

TLR4 Antibody (76B357.1) - BSA Free

(5 Reviews)

(138 Publications)

0.1 mg

NB100-56566

Immunohistochemistry: TLR4 Antibody (76B357.1) [NB100-56566] - Pericryptal Myofibroblasts are Responsible for Increased TLR4 Expression in a Subset of CRCs. Double-stained immunofluorescence for TLR4 (green) and vimentin (red) in normal (I), adenoma (II), and colon adenocarcinoma (III) (10x). In the stromal compartment of CRCs, immunofluorescent staining for TLR4 localized to the pericryptal myofibroblasts in a subset of samples. Image collected and cropped by CiteAb from the following publication (//www.jeccr.com/content/33/1/45), licensed under a CC-BY license.

Western Blot: TLR4 Antibody (76B357.1) [NB100-56566] - Analysis using 2 ug/mL on (A) human intestine and 6 ug/mL on (B) mouse intestine and (C) rat intestine lysate.

Flow (Intracellular): TLR4 Antibody (76B357.1) [NB100-56566] - Analysis using PE conjugate of NBP2-27149. An intracellular stain was performed on Jurkat cells with TLR4 antibody (76B357.1) NBP2-27149PE (blue) and an isotype control MAB004 (orange). 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. Both antibodies were conjugated to phycoerythrin.

Immunocytochemistry/Immunofluorescence: TLR4 Antibody (76B357.1) [NB100-56566] - RH-30 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-TLR4 Antibody (76B357.1) NB100-56566 at 1 ug/ml overnight at 4C and detected with an anti-mouse 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: TLR4 Antibody (76B357.1) [NB100-56566] - Immunofluorescent staining of TMAs. Representative tissue cores from normal (I), adenomatous polyps (II), and CRC (III and IV) are shown. Image collected and cropped by CiteAb from the following publication (//www.jeccr.com/content/33/1/45), licensed under a CC-BY license.

Immunohistochemistry-Paraffin: TLR4 Antibody (76B357.1) [NB100-56566] - Analysis of rat salivary gland tissue section at 1:100 dilution. The antibody generated a membrane-cytoplasmic staining in the tissue with stronger signal in ductal epithelial cells.

Immunohistochemistry-Paraffin: TLR4 Antibody (76B357.1) [NB100-56566] - Tissue section of normal human skin stained with antibody at 5 ug/mL. Membrane-cytoplasmic immunopositivity of TLR4 was primarily observed in the pigmented basel cells and the adjacent keratinocytes in the epidermal layer.

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - An intracellular stain was performed on RH30 cells with TLR4 Antibody (76B357.1) NB100-56566 (blue) and a matched mouse IgG2b Kappa isotype control (orange) MAB004. 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 Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Immunohistochemistry-Paraffin: TLR4 Antibody (76B357.1) [NB100-56566] - Human skin stained with at 5 ug/mL, peroxidase-conjugate and DAB chromogen. Staining of formalin-fixed tissues is enhanced by boiling tissue sections in 10 mM sodium citrate buffer, pH 6.0 for 10-20 min followed by cooling at RT for 20 min.

Immunohistochemistry-Paraffin: TLR4 Antibody (76B357.1) [NB100-56566] - Analysis of TLR4 in FFPE human colon tissue using an isotype control (top) and NB100-56566 (bottom) at 5 ug/mL.

Immunohistochemistry-Paraffin: TLR4 Antibody (76B357.1) [NB100-56566] - Human testis tissue stained with antibody at 5 ug/mL.

Immunohistochemistry-Frozen: TLR4 Antibody (76B357.1) [NB100-56566] - This image is TLR4(green) and nucleus(blue) at area postrema of the adult male mouse brain, x20 magnification. Primary antibody diluted 1:500. IHC-Fr image submitted by a verified customer review.

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - Analysis of formaldehyde fixed THP-1 cells (human monocytic leukemia cells) using 2 ug/10^6 cells TLR4 antibody (clone 76B357.1) with detection employing a donkey anti-mouse IgG (H+L) cross adsorbed secondary antibody, (DyLight 488 conjugated). Isotype control samples incubated with mouse IgG2b isotype control antibody were processed in parallal under the same assay conditions.

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - An intracellular stain was performed on Jurkat cells with TLR4 Antibody (76B357.1) NB100-56566 (blue) and a matched mouse IgG2b Kappa isotype control (orange) MAB004. 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 Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - An intracellular stain was performed on Raw264.7 cells with TLR4 Antibody (76B357.1) NB100-56566 (blue) and a matched mouse IgG2b Kappa isotype control (orange) MAB004. 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 Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Representative images of immunohistochemical staining of pancreatic adenocarcinoma upregulated factor (PAUF) and toll-like receptor 4 (TLR4) in human ovarian cancer specimens. The top row (A,B) represents normal ovarian tissue, middle row (C,D) shows immunoreactivity of ovarian carcinomas and the bottom row (E,F) indicates immunonegativity of ovarian caricinoma. The stromal cells of normal ovarian tissue show immunonegativity for PAUF and TLR4. The scale bar represents 100 μm.

ALWPs significantly reduced LPS-induced cell-surface levels of TLR4. (C) BV2 microglial cells were pretreated with ALWPs (500 ug/ml) or PBS for 30 min, followed by treatment with LPS (1 ug/ml) or PBS for 5.5 h. Cell-surface biotinylation was then conducted with a TLR4 antibody recognizing the N-terminal region of TLR4. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30319390), licensed under a CC-BY licence.

Effect of Cucumis sativus L. extract (CSE) on LPS induced TLR4 expression. b) Representative Western Blot of TLR4 and relative housekeeping alpha-tubulin were reported. c Expression of TLR4 protein in pAECs treated with LPS (10 ug/ml) in the presence or absence of increasing doses CSE (0.02; 0.2; 2 mg/ml); data shown are representative of at least three independent experiments and represent the mean +/- SEM. Different letters above the bars indicate significant differences (p < 0.05 ANOVA post hoc Tukey's test) Image collected and cropped by CiteAb from the following publication (//bmccomplementalternmed.biomedcentral.com/articles/10.1186/s12906-018-2254-1), licensed under a CC-BY licence.

Dasatinib affects TLR4 signaling to regulate LPS-induced proinflammatory cytokine levels in BV2 microglial cells. d) BV2 microglial cells were treated with dasatinib (250 nM) or vehicle (1% DMSO) for 30 min followed by LPS (1 ug/ml) or PBS for 5.5 h, and cell surface biotinylation was conducted. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31655606), licensed under a CC-BY licence.

Corroboration of human AKR2–protein interactions with highest confidence. (A) Representation of the components of the protein pull-down experiment using c-Myc magnetic beads with Myc-tagged human AKR2. (B) Western blot analysis of AKR2–protein interactions. Interacting proteins were incubated with AKR2 and immunopresipitated with c-Myc magnetic beads specific for the AKR2 protein tag (I) or with the c-Myc magnetic beads only as negative control (C-). Recombinant interacting proteins were included as positive control (C+). Mouse or rabbit antibodies specific for each protein were used as primary antibodies and then anti-mouse or anti-rabbit secondary antibodies were used to identify the presence of the interacting proteins (red arrow). The origin of the primary antibody is shown. (C) Corroboration of human AKR2–AKR2 interaction using protein pull-down with c-Myc magnetic beads with human Myc-tagged AKR2. The experiment was conducted as described in (B). The origin of the primary antibody and predicted size for AKR2 monomer, dimer, and trimer together with bands corresponding to fragments of the mouse anti-c-Myc antibody attached to magnetic beads are shown. (D) In order to identify unrelated proteins eluted from the c-Myc magnetic beads, a similar experiment was conducted with selected proteins but incubating only with the secondary antibody. A lane of SDS-PAGE stained with Bio-Safe Coomassie Stain corresponding to c-Myc magnetic beads alone eluted using Laemmli sample buffer was included (C--). The bands corresponding to fragments of the mouse anti-c-Myc antibody attached to magnetic beads are shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32046307), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$TDP1 depletion sensitizes glioblastoma-resistant cancer cells to temozolomide. (a) Cell lysates from RKO and DLD1 cancer cell lines were fractionated by SDS–PAGE and analyzed by immunoblotting using anti-TDP1 (Eurogentec), anti-Top1 (Santa Cruz), anti-Tubulin (Abcam) and anti-APE1 (Novus) antibodies (left). RKO and DLD1 cells were compared for their survival following exposure with the indicated doses of MMS for 15 min at 37°C (right). Data are the average of three independent experiments ± s.e.m. Where not visible, error bars are smaller than the symbol. (b) RKO cells were subjected to scrambled siRNA (Mock) or siRNA against TDP1 (TDP1KD) and cell lysates analyzed by immunoblotting (left). Control RKO (RKOSc siRNA) and RKO cells in which TDP1 levels were depleted (RKOTDP1 siRNA) were examined for their survival following exposure to the indicated doses of MMS, as described earlier in the text (right). (c) Glioblastoma multiforme T98G and U87 cancer cell lines were analyzed for methylguanine methyltransferase (MGMT) expression using anti-MGMT antibodies (Abcam) (left). High-MGMT expressing T98G cells were compared with low-MGMT expressing U87 cells for their survival following exposure to increasing concentrations of the alkylating agent temozolomide (right). (d) TG98 cells were subjected to scrambled siRNA (Mock) or siRNA against TDP1 (TDP1KD) and cell lysates analyzed by immunoblotting (left). Control T98G cells (T98GSc siRNA) and cells in which TDP1 levels were depleted (TG98TDP1 siRNA) were incubated with DMSO or 150 μM of the APE1 inhibitor CRT0044876 ‘APEi’ for 2 h followed by additional incubation with the indicated concentrations of MMS for 15 min at 37°C. Cell survival was blindly scored from three independent biological repeats, and data are the average ± s.e.m. (right). (e) Model for the repair of temozolomide-induced DNA breaks. Temozolomide delivers a methyl group to purine bases of DNA, resulting in O6-methyl guanine, N7-methyl guanine and N3-methyl adenine. The primary cytotoxic lesion is believed to be O6-methyl guanine, which can be removed by a direct repair mechanism mediated by methylguanine methyltransferase (MGMT). Inherent and acquired resistance to temozolomide via MGMT expression presents a major challenge in cancer therapy, particularly for glioblastoma multiforme. TDP1 promotes the repair of methylated purines induced by temozolomide via a distinct non-canonical BER pathway. Increasing the load of unrepaired methylated purines by exploiting the limited availability of TDP1 alone or in combination with canonical BER factors such as APE1 provides a new synthetic lethal setting to improve the clinical outcome of temozolomide-based cancer therapy. Asterisks denote statistical differences (P < 0.05; t-test) between control and TDP1-deficient cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24335147), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

OTULIN overexpression reduced the number of Iba-1+ microglial cells in the cortical ischemic penumbra in focal cerebral ischemia/reperfusion rats. A Representative images of Iba-1+ microglial cells that were morphologically classified into three types; scale bar = 10 μm. B Iba-1+ microglial cells in the ischemic penumbra and contralateral cortex of each group were detected by confocal immunofluorescence at 24 h, 72 h, and 7 days; scale bar = 75 μm. C The histogram represents the quantitative analysis of mean Iba-1 immunofluorescence intensity in each group (n = 6). Data are presented as the means ± SEMs; ###P < 0.001 versus the tMCAO group; &&&P < 0.001 versus the tMCAO+LV-Scramble group Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29544517), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

FKBP51 modulates EMT hallmarks. (a and b) FKBP51 silencing of SAN melanoma cells decreases TGF-beta and T beta RIII expression. Normalized expression rates (mean±S.D.) of TGF-beta (a, left) and T beta RIII (b, left) mRNA levels; (a, n=3; b, n=5). FKBP51 siRNA-treated sample expression=1. Western blot assay of TGF-beta in SAN melanoma cells treated with nonsilencing (NS) RNA or FKBP51 siRNA (a, right). Flow cytometric analysis of T beta RIII (endoglin) expression (b, right): FKBP51 siRNA-treated cells moved to the left relative to NS RNA-treated cells because of reduced staining (MFI: 111±10 and 64±3 in NS RNA and FKBP51 siRNA-treated cells, respectively). (c, and d) FKBP51 overexpression enhances TGF-beta and T beta RIII expression. Normalized expression of TGF-beta (c, left) and T beta RIII (d, left) mRNA in WT, EV-, or FKBP51-stably transfected melanoma cells. WT sample expression=1. (c, n=3; d, n=5). Western blot assay of TGF-beta levels in the same cells (c, right). Anti-Flag-labelled exogenous FKBP51. Flow cytometric analysis of T beta RIII expression (d, right). FKBP51-overexpressing cells moved to the right relative to WT or EV cells, indicating increased expression. (e) Graphic representation of cell counts ( × 10−3) in WT, EV-, or FKBP51-stably transfected melanoma cell cultures. Results are means of six independent experiments each performed in triplicate. (f) FKBP51 upregulates colony number and size. Colonies were counted under low magnification ( × 10) at four points on each dish. The data represent the means of two independent experiments performed in triplicate. Magnification: upper, × 10; lower × 40. (g) Boyden chamber filters invaded by melanoma cells. Filter was stained with Crystal Violet. OD value was obtained by reading the eluted Crystal Violet with a spectrophotometer at a wavelength of 570 nm. The increased OD in FKBP51 samples indicated that FKBP51-overexpressing cells invaded matrigel more efficiently than control cells. The data represent the means of three independent experiments performed in triplicate Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/cddis2013109), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Functional assessment of Fanconi anemia pathway. (a) The experimental scheme for MMC treatment. Twenty‐four hours after plating, cells were cultured with or without MMC 1 μM for an additional 24 hr, after which the cells were harvested for western blot or immunostaining. (b) Western blot with FANCD2 antibody of BJ, proband fibroblasts, FANCB mutant (null) fibroblasts and FANCD2 mutant (null) fibroblasts. (c) Western blot with FANCD2 antibody of non‐FA control lymphoblasts (LCL), proband LCL‐A‐2017, proband LCL‐B‐2017, FANCB mutant (null) LCL, and FANCD2 mutant (null) LCL. (d) Representative figures of FANCD2 foci formation in the indicated cells. (e) Quantification of FANCD2 foci formation following treatment with or without 1 μM MMC. Experiments were performed in triplicate. One hundred cells were counted for each experiment Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29193904), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Pot1a prevents DDR in HSCs. a, b Telomeric DDR in 8 week-old LSK cells upon Pot1a knockdown. a Immunocytochemical staining of TRF1 (green) and 53BP1 (red). Foci co-stained with TRF1 and 53BP1 were identified as TIFs. Nuclei were stained with TOTO3 (blue). Scale bar, 2 μm. b Frequency of TIFs per cell after 1 week of culture. Data are expressed as the mean ± SD (n = 100, *p < 0.01 by t-test). Representative data from three independent experiments are shown. c–f Telomeric DDR in donor-derived control-GFP or Pot1a overexpressing 8 week-old LSK cells 4 months post BMT. c Immunocytochemical staining of TRF1 (green) and 53BP1 (red). Nuclei were stained with TOTO3 (blue). Scale bar, 2 μm. d Frequency of TIFs per cell. Data are expressed as the mean ± SD (n = 120, *p < 0.01 by t-test). Representative data from 3 independent experiments are shown. e Immunocytochemical staining of TRF1 (green) and RPA32 (red). f Immunocytochemical staining of TRF1 (green) and pChk1 (red). Scale bar, 2 μm. g Flow cytometric analysis of Chk1 and pChk1 in donor-derived GFP+ LSKCD48–CD150+ cells after 5 months of 2nd BMT. Mean fluorescence intensity of Chk1 and pChk1 (left panels). Data are expressed as the mean ± SD (n = 3, *p < 0.01 by t-test). Representative FACS profiles of Chk1 and pChk1 in donor-derived GFP+ LSKCD48–CD150+ cells (right panels) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28986560), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Lamin A/C-53BP1 interaction is regulated in a DNA damage-dependent manner. (A) Left; HDF were subjected to IR (10 Gy) and allowed to recover for 1 h. Association between A-type lamins and 53BP1 was assessed by immunoprecipitation of endogenous lamin A/C followed by immunoblotting with 53BP1 and lamin A/C antibodies. WCE, whole cell extract, IP: immunoprecipitates. WCE represents 5% input. Right; endogenous lamin A/C was immunoprecipitated and supernatants or pellets were analysed by immunoblotting for interaction with JMJD2A. (B) U2OS/GFP-lamin A cells were pretreated with caffeine (20 mm) for 1 h before exposure to IR (10 Gy, 1 h recovery). Cell extracts were then subjected to immunoprecipitation using GFP-Trap beads, and bound complexes were then analysed by immunoblotting using 53BP1 and GFP antibodies. WCE represents 1% input. (C) As in (C) except cells were pretreated with 10 μm ATMi for 1 h before IR. WCE represents 1% input. (D) U2OS/GFP-lamin A cells were subjected to laser micro-irradiation, fixed 1 h later and immunostained with gamma -H2AX antibody. Scale bar, 10 μm. (E) U2OS cells were transfected with siCTRL or siLMNA and subjected to laser micro-irradiation, fixed 15 min later and then processed for immunofluorescence with gamma -H2AX and 53BP1 antibodies. Scale bar, 10 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25645366), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ma, Pm, ChHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ma, Pm, ChHa

Applications:

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

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

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-5031A

Alt Catalog# IMG-5031A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-27149AF350
Alexa Fluor 405	NBP2-27149AF405
Alexa Fluor 488	NBP2-27149AF488
Alexa Fluor 532	NBP2-27149AF532
Alexa Fluor 594	NBP2-27149AF594
Alexa Fluor 647	NBP2-27149AF647
Alexa Fluor 700	NBP2-27149AF700
Alexa Fluor 750	NBP2-27149AF750
Allophycocyanin	NBP2-27149APC
Allophycocyanin/Cy7	NB100-56566APCCY7
Biotin	NBP2-27149B
DyLight 350	NBP2-27149UV
DyLight 405	NBP2-27149V
DyLight 488	NBP2-27149G
DyLight 550	NBP2-27149R
DyLight 594	NB100-56566DL594
DyLight 650	NBP2-27149C
DyLight 680	NBP2-27149FR
DyLight 755	NBP2-27149IR
FITC	NBP2-27149F
HRP	NBP2-27149H
Janelia Fluor 549	NB100-56566JF549
Janelia Fluor 646	NB100-56566JF646
PE	NBP2-27149PE
PE/Atto594	NB100-56566PEATT594
PE/Cy5.5	NB100-56566PECY55
PE/Cy7	NB100-56566PECY7
PerCP	NBP2-27149PCP
mFluor Violet 450 SE	NBP2-27149MFV450
mFluor Violet 500 SE	NBP2-27149MFV500
mFluor Violet 610 SE	NBP2-27149MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Azide Free	NBP2-27149
BSA Free	NB100-56566SS
Azide Free	NBP2-27149SS

compare

(select up to 3 products from this page to compare)

NB100-56576

SARS Nucleocapsid Protein Antibody - BSA Free

(149 Publications)

0.1 mg

NB100-56576

<b>Orthogonal Strategies Validation. </b>Dual RNAscope ISH-IHC: SARS Nucleocapsid Protein Antibody [NB100-56576] - Formalin-fixed paraffin-embedded tissue sections of SARS-CoV-2 infected human lung tissue were probed for SARS-CoV-2 viral RNA (ACD anti-sense specific probe v-nCoV2019-S (848561); Fast Red chromogen, ACD [322360]). Adjacent tissue section was processed for immunohistochemistry using rabbit polyclonal anti-SARS Nucleocapsid Antibody [NB100-56576] at 15ug/mL with 1 hr incubation at 25 degrees Celsius followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody [VC003] and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to SARS-CoV-2 infected cells.

Immunohistochemistry: SARS Nucleocapsid Protein Antibody [NB100-56576] - Characteristics of 2B4 cells clonally derived from human bronchial epithelial Calu-3 cells. Finally, 2B4 cells (passage 6) were infected with SARS-CoV (MOI = 0.1) for 24, 48, and 72 hrs before being fixed with 4% paraformaldehyde for monitoring the morphological changes of infected cells, as visualized by the expression of SARS-CoV NP protein (red) by using the standard IHC (F). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0008729) licensed under a CC-BY license.

Western Blot: SARS Nucleocapsid Protein Antibody [NB100-56576] - Western blot shows recombinant SARS-CoV-2 Nucleocapsid protein. PVDF membrane was probed with 1 ug/mL of Rabbit Anti-SARS-CoV-2 Nucleocapsid Polyclonal Antibody (Catalog # NB100-56576) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). A specific band was detected for SARS-CoV-2 Nucleocapsid at approximately 55 kDa (as indicated). This experiment was conducted under reducing conditions and using Western Blot Buffer Group 1

Western Blot: SARS Nucleocapsid Protein Antibody [NB100-56576] - analysis of SARS Nucleocapsid in (A) untransfected mouse melanoma cell lysate and (B) transfected cell lysate using this antibody.

Reactivity:

V, V, V-Vi

Species Glossary

Reactivity: V, V, V-Vi

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-548

Alt Catalog# IMG-548

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-56576AF350
Alexa Fluor 405	NB100-56576AF405
Alexa Fluor 488	NB100-56576AF488
Alexa Fluor 532	NB100-56576AF532
Alexa Fluor 700	NB100-56576AF700
Alexa Fluor 750	NB100-56576AF750
Allophycocyanin	NB100-56576APC
Biotin	NB100-56576B
DyLight 350	NB100-56576UV
DyLight 405	NB100-56576V
DyLight 488	NB100-56576G
DyLight 550	NB100-56576R
DyLight 594	NB100-56576DL594
DyLight 650	NB100-56576C
DyLight 680	NB100-56576FR
DyLight 755	NB100-56576IR
FITC	NB100-56576F
HRP	NB100-56576H
Janelia Fluor 549	NB100-56576JF549
Janelia Fluor 646	NB100-56576JF646
PE	NB100-56576PE
PerCP	NB100-56576PCP
mFluor Violet 450 SE	NB100-56576MFV450
mFluor Violet 500 SE	NB100-56576MFV500
mFluor Violet 610 SE	NB100-56576MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56576SS

compare

(select up to 3 products from this page to compare)

NB100-309

ATM Antibody (2C1)

(3 Reviews)

(130 Publications)

100 ul

NB100-309

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

Hu, Mu, Rt, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Pm

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Validated by:

Validated by:

compare

(select up to 3 products from this page to compare)

NBP2-36488

PINK1 Antibody (8E10.1D6) - BSA Free

(8 Publications)

0.1 mg

NBP2-36488

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: PINK1 Antibody (8E10.1D6) [NBP2-36488] - HeLa cells were treated with valinomycin (1 uM, 24h) prior to being fixed in 10% buffered formalin for 10 min and permeabilized in 0.1% Triton X-100 in PBS for 10 min. Cells were incubated with NBP2-36488 at 50 ug/ml for 1hr at room temperature, washed 3x in PBS and incubated with Alexa-DyLight-488 anti-mouse secondary antibody. PINK1 (Green) was detected at the mitochondria. Tubulin (Red) was detected using an anti-tubulin antibody with an anti-rabbit DyLight 550 secondary antibody. DNA (Blue) was counterstained with DAPI. Note: mitochondria staining might not be easily observed without treatment with valinomycin or CCCP. Image objective 40x.

<b>Biological Strategies Validation. </b>Western Blot: PINK1 Antibody (8E10.1D6) [NBP2-36488] - Whole cell protein from HeLa cells treated with or without valinomycin (1 uM, 24h) as indicated was separated by SDS-PAGE on a 7.5% polyacrylamide gel. Protein was transferred to PVDF membrane and probed with 2 ug/ml anti-PINK1 in 1% BSA and detected with an HRP-conjugated anti-mouse secondary antibody using chemiluminescence. PINK1 is seen to be upregulated with treament and with a molecular weight at approximately 60 kDa.

Western Blot: PINK1 Antibody (8E10.1D6) [NBP2-36488] - Analysis of (A) Partial Recombinant Human PINK-1 protein with estimated molecular weight at 13kDa and (B) Human Liver lysate using PINK1 antibody clone 8E10.1D6 at 3ug/ml concentration, molecular weight ~64 kDa.

Regulation of the mitophagic marker PINK1 in WT and TLR4 KO mice. c) Expression of PINK1 was assessed by Western blotting. The PINK1 protein levels were significantly increased in the ipsilateral side compared with the contralateral side in WT mice, and no significant difference was shown in TLR4 KO mice. Image collected and cropped by CiteAb from the following publication (//molecularbrain.biomedcentral.com/articles/10.1186/s13041-018-0354-y), licensed under a CC-BY licence.

Anti-tumor activity of regorafenib and SC-78 in a murine TNBC metastasis model.(A) Nude mice were subcutaneously injected with MDA-MB-468 cells (2 × 106). Mice were treated with vehicle, bevacizumab (125 μg/100 μl, twice a week, IP), regorafenib, or SC-78 (10 mg/kg, everyday, oral) for 43 days (n = 6), and the tumor size (left, bottom) was measured. In vivo protein levels were analyzed (Middle, top). Middle, bottom, the in vivo SHP-1 activity. Right, Representative images of IHC staining (100 × ). *p < 0.05, **p < 0.01. (B) Luciferase-expressing MDA-MB-231 (1 × 106) cells were injected orthotopically into the mammary fat pad of the mice. After two weeks, mice received regorafenib and SC-78, or vehicle orally at 10 mg/kg/every day (n = 5). Tumor growth was monitored by IVIS imaging system at the indicated times. Left, top, visualized by IVIS analysis. Left, bottom, quantification analysis from the IVIS total flux. Right, Representative images of IHC staining (100×). *p < 0.05, **p < 0.01. (C) In vivo bioluminescence images of nude mice injected i.v. with MDA-MB-231/Luc2 cells (1 × 106). After bioluminescence was observed, mice received vehicle or SC-78 orally at 10 mg/kg/every day. left, visualized by IVIS analysis. Right, Kaplan–Meier plot showing animal survival after treatment with vehicle or SC-78 (n = 8). The survival endpoint was set at 64 days after drug administration. (D) Schematic displays the drug mechanism of regorafenib and SC-78 on VEGF-A autocrine and paracrine inhibition and cell migration. SC-78 suppressed cancer metastasis dominantly through SHP-1 dependent-STAT3 dephosphorylation. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27364975), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Pm

Applications:

, , , ,

Applications: , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-36488AF350
Alexa Fluor 405	NBP2-36488AF405
Alexa Fluor 488	NBP2-36488AF488
Alexa Fluor 532	NBP2-36488AF532
Alexa Fluor 594	NBP2-36488AF594
Alexa Fluor 647	NBP2-36488AF647
Alexa Fluor 700	NBP2-36488AF700
Alexa Fluor 750	NBP2-36488AF750
Allophycocyanin	NBP2-36488APC
Biotin	NBP2-36488B
DyLight 350	NBP2-36488UV
DyLight 405	NBP2-36488V
DyLight 488	NBP2-36488G
DyLight 550	NBP2-36488R
DyLight 594	NBP2-36488DL594
DyLight 650	NBP2-36488C
DyLight 680	NBP2-36488FR
DyLight 755	NBP2-36488IR
FITC	NBP2-36488F
HRP	NBP2-36488H
Janelia Fluor 549	NBP2-36488JF549
Janelia Fluor 646	NBP2-36488JF646
PE	NBP2-36488PE
PerCP	NBP2-36488PCP
mFluor Violet 450 SE	NBP2-36488MFV450
mFluor Violet 500 SE	NBP2-36488MFV500
mFluor Violet 610 SE	NBP2-36488MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-36488SS
Azide and BSA Free	NBP2-80910

compare

(select up to 3 products from this page to compare)

NBP1-77080

NLRP3/NALP3 Antibody - BSA Free

(2 Reviews)

(30 Publications)

0.1 mg

NBP1-77080

Immunohistochemistry-Paraffin: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - Analysis of NALP3 in mouse lung tissue using anti-NALP3 antibody. Image from verified customer review.

Western Blot: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - Analysis of NALP3 in K562 cell lysate with NALP3 antibody at 1 ug/mL (A) in the absence and (B) in the presence of blocking peptide.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - hADSC-Evs suppressed NLRP3 inflammasome activation in ocular surface of experimental mice under desiccating stress. Representative image of immunofluorescent staining of NLRP3 related genes in corneal and conjunctival epithelia of desiccating mice or treated with hADSC-EVs (*conjunctiva; open triangle cornea). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32884023/) licensed under a CC-BY license.

hADSC-Evs suppressed NLRP3 inflammasome activation in ocular surface of experimental mice under desiccating stress. (A) Representative image of immunofluorescent staining of NLRP3 related genes in corneal and conjunctival epithelia of desiccating mice or treated with hADSC-EVs (*conjunctiva; open triangle cornea). (B,C) qRT-PCR showed the mRNA levels of NLRP3 related genes in conjunctiva and cornea (four corneas/conjunctivas were mixed as a sample). Data was shown as mean ± SEM. *p < 0.05.

IFI16 inhibits c-Myc-stimulated transcription and hTERT expression in HeLa cells.(A) Total protein extracts prepared from HeLa cells infected with control retrovirus (lane 1) or a virus encoding IFI16 protein (lane 2) were subjected to immunoblotting using antibodies specific to the indicated proteins. (B) Sub-confluent cultures of HeLa cells were transfected with pMyc-TA-luc reporter plasmid (1.0 µg) along with a second pRL-TK reporter plasmid (0.2 µg) and an empty plasmid (pCMV; column 1), a plasmid encoding c-Myc (column 2 and 4), a plasmid encoding IFI16 (column 3), or both plasmids encoding c-Myc and increasing amounts of the plasmid encoding IFI16 protein (column 5 and 6). After 44–48 h of transfections, cells were lysed and the lysates were analyzed for dual luciferase activity. Normalized relative luciferase activity in control cells is indicated as 1.0. (C) Total protein extracts prepared from HeLa cells infected with control retrovirus (lane 1) or a virus encoding antisense to IFI16 mRNA (lanes 2) were subjected to immunoblotting using antibodies specific to the indicated proteins. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0008569), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ec

Species Glossary

Reactivity: Hu, Mu, Ec

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	NBP1-77080AF350
Alexa Fluor 405	NBP1-77080AF405
Alexa Fluor 488	NBP1-77080AF488
Alexa Fluor 532	NBP1-77080AF532
Alexa Fluor 594	NBP1-77080AF594
Alexa Fluor 647	NBP1-77080AF647
Alexa Fluor 700	NBP1-77080AF700
Alexa Fluor 750	NBP1-77080AF750
Allophycocyanin	NBP1-77080APC
Biotin	NBP1-77080B
DyLight 350	NBP1-77080UV
DyLight 405	NBP1-77080V
DyLight 488	NBP1-77080G
DyLight 550	NBP1-77080R
DyLight 594	NBP1-77080DL594
DyLight 650	NBP1-77080C
DyLight 680	NBP1-77080FR
DyLight 755	NBP1-77080IR
FITC	NBP1-77080F
HRP	NBP1-77080H
Janelia Fluor 549	NBP1-77080JF549
Janelia Fluor 646	NBP1-77080JF646
PE	NBP1-77080PE
PerCP	NBP1-77080PCP
mFluor Violet 450 SE	NBP1-77080MFV450
mFluor Violet 500 SE	NBP1-77080MFV500
mFluor Violet 610 SE	NBP1-77080MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-77080SS

compare

(select up to 3 products from this page to compare)

NB910-40435

LC3 Antibody Pack

(3 Reviews)

(14 Publications)

1 Pack

NB910-40435

<b>Genetic Strategies Validation. </b>Knockout Validated: LC3 Antibody Pack [NB910-40435] - LC3B was detected in immersion fixed Cloroquine treated HeLa cells (left) but was not detected in LC3B knockout HeLa cells (right) using rabbit anti-human LC3B polyclonal antibody (Catalog #NB100-2220) at 0.3 ug/mL for 3 hours at room temperature. Cells were stained using the NorthernLights(TM) 557-conjugated anti-Rabbit IgG Secondary Antibody (red; Catalog # NL004) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm.

<b>Biological Strategies Validation. </b>Western Blot: LC3 Antibody Pack [NB910-40435] - High autophagosome concentration is consumed during early immortalized human mesenchymal stem cell differentiation. Immortalized human mesenchymal stem cells were differentiated under osteogenic conditions (see Materials and methods) and assayed for changes in LC3I and LC3II during a 72-hour window. Cells were differentiated under standard conditions (top) or with addition of 5 uM rapamycin (middle) or 5 nM bafilomycin (bottom) for the first 3 hours of differentiation to modulate autophagy. Immunoblots were performed for LC3 at the indicated time points to assess autophagosome degradation via relative changes in LC3II (lower band; 17 kDa). Studies were repeated three times with similar trends seen consistently. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license. LC3A Antibody [NB100-2331]

Immunohistochemistry: LC3 Antibody Pack [NB910-40435] - Localization of LC3 by immunohistochemical method. The immunohistochemical staining shows that LC3, CRF, and HIF-1alpha have an overlapping localization in villous and extravillous trophoblast. d: decidua; v: villi; DeVe: decidual vessel. Original magnification 40x. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2013/689768/) licensed under a CC-BY license. LC3B Antibody [NB100-2220]

Immunohistochemistry: LC3 Antibody Pack [NB910-40435] - Brain, Cerebral Cortex, Cell Processes in Gray Matter 40x.

Immunohistochemistry: LC3 Antibody Pack [NB910-40435] - Analysis in PFA fixed NIH/3T3 cells using anti-LC3A antibody. Image from verified customer review. LC3A Antibody [NB100-2331]

Reactivity:

Hu, Mu, Rt, Po, Al, Am, Av, Ba, Bv, Ca, Ch, ChHa, Fi, Gp, Ha, In, Pl, Pm, Pm, Rb, SyHa, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Al, Am, Av, Ba, Bv, Ca, Ch, ChHa, Fi, Gp, Ha, In, Pl, Pm, Pm, Rb, SyHa, Ze

Applications:

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

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

Validated by:

Validated by:

compare

(select up to 3 products from this page to compare)

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

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Lysate Life Stage

Lysate Protein State

Lysate Subcellular Fraction

Lysate Tissue

Lysate Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

LC3B Antibody - BSA Free

HIF-2 alpha/EPAS1 Antibody - BSA Free

Collagen I Antibody

PINK1 Antibody - BSA Free

Nbs1 Antibody

CHREBP Antibody - BSA Free

TLR4 Antibody (76B357.1) - BSA Free

SARS Nucleocapsid Protein Antibody - BSA Free

ATM Antibody (2C1)

PINK1 Antibody (8E10.1D6) - BSA Free

NLRP3/NALP3 Antibody - BSA Free

LC3 Antibody Pack