Lipid-and-Metabolism reagents: Novus Biologicals

NB100-123

HIF-1 alpha Antibody (H1alpha67)

(9 Reviews)

(165 Publications)

0.1 ml

NB100-123

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - MLN4924 induces accumulation of HIF1a in a time dependent manner. Cells were treated with 0.1uM MLN4924 for indicated time periods, followed by IB with indicated antibodies. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2012125) licensed under a CC-BY license.

Immunohistochemistry: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Analysis of HIF-1 alpha in human lung tissue. Image courtesy of product review by Aneta Gandjeva.

Immunoprecipitation: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - MG132 attenuates the inhibitory effect of interleukin-1beta on HIF-1/AM axis. U87MG cells were incubated for 2 h in hypoxia (1% O2) with or without interleukin-1beta (10 ng/ml). The proteasome inhibitor MG132 was added 30 min in advance to prevent ubiquitinated HIF-1alpha from proteasomal degradation. HIF-1alpha was precipitated by anti-HIF-1alpha antibody. Ubiquitin was detected by immunoblotting. Non-specific mouse IgG was used as a negative control. The results are representative for three independent experiments Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2013562) licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Analysis using the HRP conjugate of NB100-123. Detection of HIF-1 alpha in cobalt chloride treated/untreated COS-7 nuclear extracts using NB100-123.

$<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Analysis using the HRP conjugate of NB100-123. On day 1, MEF cells (+/+,-/-), were grown on 15cm dish (2x10 to the 6th cells). On day 2, cells were exposed to hypoxia for 4hrs. Cells were washed with ice cold PBS twice and whole cell protein was extracted extracted with RIPA buffer fortified with protease. Upon quantification, 100ug of protein was fractionated on 7% polyacralymide gel. Gel was transferred overnight onto nitrocellulose membrane. The membrane was probed with HIF-1 alpha monoclonal antibody at a 1:500 dilution (NB100-123). The secondary antibody was conjugated with HRP and was used at a 1:2500 dilution. Photo courtesy of Dr. Gregg Semenza, Johns Hopkins University.$

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Dapagliflozin protects against metabolic switch by inhibition of HIF-1 alpha. Representative images of PTCs incubated with 10 umol/l of molidustat for 6 h with immunofluorescent staining for HIF-1 alpha. Scale bar = 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33187129/) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Immunohistochemical detection of HIF-1alpha protein in human tissues. The nature of the tissue is indicated on top of each figure. Original magnifications are as follows: A, x400; B, x400; C, x100; D, x100; E, x100; F, x100; G, x40; H, x40. Image collected and cropped by CiteAb from the following publication (//bmcgenet.biomedcentral.com/articles/10.1186/1471-2156-5-27), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Staining in pig endothelial cells under hypoxia condition using NB100-123. Image from verified customer review.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Staining on pig tissue (brown) using NB100-123. Image from verified customer review.

Immunohistochemistry: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Staining of biotin conjugated HIF-1 alpha (NB100-123B) in human kidney.

Immunoprecipitation: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Immunoprecipitation of HIF-1alpha using NB100-123 in COS7 CoCl2 treated lysate. Heavy and light chains are also detected. Image using the HRP form of this antibody.

Immunohistological and western blot analyses of HIF-1 alpha .(A) PAB liver stained by HIF-1 alpha (original magnification, ×20). (B) Sham-operated control liver stained by HIF-1 alpha (original magnification, ×20). (C) Enlarged view of the boxed area in the Image (A) (original magnification, ×100). (D) Western blot analysis of HIF-1 alpha (mean ± SEM), * P<0.05. HIF-1 alpha : hypoxia-inducible factor-1 alpha ; PAB: pulmonary artery banding.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Mouse Monoclonal HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Images of HIF-1 alpha localization (red) in CTR and CoCl2-treated oAECs after 24 h of culture. Image from a verified customer review.

Western Blot: Mouse Monoclonal HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Image of HIF-1 alpha activation in AECs control cells (CTR) and after 24h of 10 and 50µM of CoCl2-treatment; HIF-1 alpha time course at shorter CoCl2 incubation times. Image from a verified customer review.

Immunohistochemistry: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - 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 & cropped by CiteAb from the following publication (//bmcgenet.biomedcentral.com/articles/10.1186/1471-2156-5-27), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Immunohistological & western blot analyses of HIF-1 alpha .(A) PAB liver stained by HIF-1 alpha (original magnification, ×20). (B) Sham-operated control liver stained by HIF-1 alpha (original magnification, ×20). (C) Enlarged view of the boxed area in the Image (A) (original magnification, ×100). (D) Western blot analysis of HIF-1 alpha (mean ± SEM), * P<0.05. HIF-1 alpha : hypoxia-inducible factor-1 alpha ; PAB: pulmonary artery banding. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26863419), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Analysis of CBF treatment in HCT116 implanted mouse models & tumour tissue samples. (a) Tumour size versus CBF treatment. The lowest tumour growth rate was found in i.p. group during CBF treatment. (b) Analysis of HIF-1 alpha mRNA level in tumour tissues. There was a significant upregulated HIF-1 alpha level in i.p. group. Results are means with standard errors from 4 replicates. (c) Inhibition of HIF-1 alpha nuclear translocation in the i.t. sample. CBF strongly inhibited HIF-1 alpha nuclear accumulation in the tumour of xenografts implanted with HCT116 cells. Scale bars equal 10 μm. White arrows: HIF-1 alpha in the cytosol. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23818933), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - CycT alleviates tumor hypoxia. The effects of CycT on the levels of exogenous hypoxia-marker pimonidazole labeling (A), the levels of hypoxia-inducible CA9 enzyme (B), & the levels of hypoxia-inducible factor HIF1 alpha (C) in orthotopic tumor xenografts. Scale bar: Montage, 1 mm; 10X, 20 μm. Data are plotted as mean ± SEM. For statistical analysis, the levels in treated tumors were compared to the levels in control tumors with a Welch 2-sample t-test. **p-value < 0.005. IHC images are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30723259), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Schematic demonstration of the three HIF1 alpha antibodies used in this study & their epitopes (Figs. 2a & b). Ab1 is a polyclonal antibody raised against N-domain of wild type HIF1 alpha & does not recognize HIF1 alpha 1.2 due to it's different N-terminal part (Fig. 2a). Ab2 & Ab3 are monoclonal & polyclonal antibodies, respectively, with epitopes in the common parts of HIF1 alpha & HIF1 alpha 1.2 (Fig.2a & b). Immunohistochemical analysis performed on thin adjacent sections of NE-differentiated prostate cancer using the HIF1 alpha antibodies Ab1 (Fig. 2c), Ab 2 (Fig. 2d), Ab 3 (Fig. 2e) & HIF1 beta antibody (Fig. 2f). Immunopositivity was detected for HIF1 alpha with Ab2 & Ab3 while HIF1 alpha Ab1 produced no detectable staining. HIF1 beta was also positive in adjacent section (Fig. 2f). Double staining of chromogranin A & androgen receptor antigens on adjacent sections (Fig. 2g) showed immunopositivity for chromogranin A (Fast red). Androgen receptor antibody (DAB, brown) produced no staining. Immunostaining of benign prostate tissue with HIF1 alpha Ab3 showed immunopositivity in NE-like cells of benign prostate tissue (Fig. 2h). In addition, HIF1 beta antibody recognized benign NE-like cells in benign prostate hyperplasia (Fig. 2i). Double staining with HIF1 alpha Ab3 & HIF1 beta (Fig. 2j) shows co-localization of the two proteins in NE-like cells of benign prostate hyperplasia (HIF1 alpha Ab3 red stain, HIF1 beta brown stain). Panels a, b, c, d, e, f & g: 40× objective. Panels h, i & j: 60× objective. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20663134), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - 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) & 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 & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/2051-5960-2-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Levels of GSH in cortical neurons exposed to hypoxia. A) During hypoxia, GSH increased in MAP2-ir neurons with round somata (bottom panel, open arrow) & decreased in neurons with pyramidal-like morphology (upper panel, solid arrow). B) GSH increased in a subset of GAD65/67–ir neurons exposed to hypoxia (bottom panel, open arrow). C) Elevated HIF-1 alpha expression in GAD65/67–ir neurons containing high levels of GSH when exposed to hypoxia (middle panel). BSO treatment decreased HIF-1 alpha expression in GAD65/67-positive neurons during hypoxia. D) Percentages of HIF-1 alpha -expressing GAD65/67-ir neurons expressing a high level of GSH & GAD65/67-ir neurons expressing a low levels of GSH & HIF-1 alpha (mean ± SD; n = 3). The “low” level referred to the level of GSH in normoxic GAD65/67 neurons that was normalized to 1. The “high” level referred to the elevated GSH level in GAD65/67 neurons with a mean of 1.40 ± 0.10. E) Total MCB-GSH intensity in GAD65/67-positive neurons with & without BSO after hypoxia (mean ± SD; 8-10 neurons quantified from each experiment, n = 3 independent cultures). Scale bars, 20 μm. Image collected & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/2051-5960-2-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - Results of in situ hybridization & immunohistochemistry on thin adjacent section to detect expression of HIF-1 alpha 1.2 mRNA & HIF1 alpha protein in malignant & benign prostate tissue. In situ hybridization (antisense probe, Fig. 3a) & immunostaining with HIF1 alpha Ab2 (Fig. 3c) on thin adjacent sections of NE-differentiated prostate adenocarcinoma showed co-localization of HIF1 alpha 1.2 transcript & HIF-1 alpha protein. Incubation with sense probe did not generate any detectable hybridization signals (Fig. 3b). Both In situ hybridization (Fig. 3d antisense) & HIF-1 alpha Ab2 immunostaining (Fig. 3f) were negative in non-NE-differentiated prostate adenocarcinoma. In situ hybridization with sense probe performed on non-NE-differentiated prostate cancer (Fig. 3e) was negative. In situ hybridizering on benign prostate tissue showed HIF1 alpha 1.2 transcript in NE-like cells of benign prostate tissue (Fig. 3g, ↗). The sense probe on thin adjacent section generated no signals (Fig. 3h,↗). Furthermore, co-localization of HIF1 alpha 1.2 transcript (Fig. 3i,↗,◢,↖) & HIF1 alpha protein, detected with HIF1 alpha Ab3 (Fig. 3j,↗,◢,↖) was also shown in NE-like cells of benign prostate tissue. Panels a, b, c, d, e, f, g, h, i, j: 40× objective. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20663134), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - HX-induced Sirt1 expression in white matter OPCs requires HIF1 alpha .(a) HIF1 alpha stabilization of Sirt1 transcript expression in OPCs as revealed by representative RT–PCR represents higher level of Sirt1 mRNA in VHL cKO mice. GDPDH mRNA serves as a control. Mean±s.e.m., n=3 brains for each group. (b,c) Representative western blot demonstrates a transient increase of HIF1 alpha expression in HX white matter at P18 with no significant effect at P11 (P=0.7955) & P45 (P=0.7333). Histograms show mean±s.e.m. (d,e) Graphs represent the percentages of Sirt1+Ki67+ & NG2+Ki67+ cells after HX white matter in WT & HIF1 alpha KO mice. Number in parentheses within bar indicates number of samples (n=4 brains per group & per genotype; ****P<0.0001, one-way analysis of variance, Bonferroni post hoc test, mean±s.e.m.). (f,g) Western blot demonstrates no increase (P=0.8231) in Sirt1 & HIF1 alpha expression in white matter of Hif1 alpha KO mice. Actin was used as loading control (mean±s.e.m.; n=3 brains for each experiment, group & genotype). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms13866), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody (H1alpha67) [NB100-123] - HIF-1 alpha expression in primary cortical neurons exposed to hypoxia/ischemia. A & A’) Neurons were double-stained for HIF-1 alpha & MAP2 in the presence of 5 & 25 mM glucose with & without hypoxia. HIF-1 alpha expression in the somata was observed in cells with interneuron-like morphology after hypoxia. B) CoCl2 (0.3 mM) induced HIF-1 alpha expression in cells with interneuron-like morphology. C) Quantification represents the increase in HIF-1 alpha –ir staining (mean ± SD; 5-10 neurons quantified from each experiment, n = 3 experiments). D)In vivo brain slice shows a similar pattern of positive HIF-1 alpha -ir in round soma (open arrow) & negative in neurons with pyramidal-like morphology (solid arrow) in the ipsilateral side. *p < 0.05, compared with normoxia (25 mM glucose), #p < 0.05, compared with hypoxia (25 mM glucose). Scale bars, 20 μm (A, A’, B); 10 μm (D). Image collected & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/2051-5960-2-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Av, Bv, Ca, Ma, Pm, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Av, Bv, Ca, Ma, Pm, Rb, Sh

Applications:

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

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

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-123AF350
Alexa Fluor 405	NB100-123AF405
Alexa Fluor 488	NB100-123AF488
Alexa Fluor 532	NB100-123AF532
Alexa Fluor 594	NB100-123AF594
Alexa Fluor 647	NB100-123AF647
Alexa Fluor 700	NB100-123AF700
Alexa Fluor 750	NB100-123AF750
Allophycocyanin	NB100-123APC
Biotin	NB100-123B
CoraFluor 1	NB100-123CL1
DyLight 350	NB100-123UV
DyLight 405	NB100-123V
DyLight 488	NB100-123G
DyLight 550	NB100-123R
DyLight 594	NB100-123DL594
DyLight 650	NB100-123C
DyLight 680	NB100-123FR
DyLight 755	NB100-123IR
FITC	NB100-123F
HRP	NB100-123H
Janelia Fluor 525	NB100-123JF525
Janelia Fluor 669	NB100-123JF669
PE	NB100-123PE
PerCP	NB100-123PCP
mFluor Violet 450 SE	NB100-123MFV450
mFluor Violet 500 SE	NB100-123MFV500
mFluor Violet 610 SE	NB100-123MFV610

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NB400-135

CHREBP Antibody - BSA Free

(7 Reviews)

(158 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>Western Blot: 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.

$Immunoblot analysis of livers from control & L-Chrebp−/− mice subjected to fasting & refeeding with a high-sucrose diet. Littermate control & L-Chrebp−/− mice (same as those described in supplemental Tables S2A & S2B) were subjected to fasting & refeeding. The nonfasted (N) groups were fed chow diet ad libitum. The fasted (F) group was fasted 12 h, & the refed (R) group was fasted for 12 h & then refed with 60% (w/w) high-sucrose diet for 12 h prior to study. Liver whole-cell lysates & membrane fractions were prepared individually, & equal amounts of protein from each mouse of the same group (four per group) were pooled. Aliquots (40 μg for whole-cell lysates & 30 μg for membrane fractions) of the pooled protein were subjected to SDS-PAGE & immunoblot analysis. Immunoblot analysis of Insig-1 & Insig-2 were carried out using membrane fractions. Whole-cell lysates were used to detect other proteins. The precursor & nuclear forms of SREBPs are denoted as P & N, respectively. Calnexin was used as loading control. Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0022227520331369), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Raffinose stimulates transcription of genes involved in epidermal barrier function in HaCaT cells.(a & b) HaCaT cells were treated with vehicle, 1 μM or 10 μM raffinose (Raf), or 1 μM TO901317 (T17) for 24 h. Expressions of transcripts (a) & 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, siLXR alpha , or siLXR beta , & then treated with 1 μM raffinose for 24 h. Expression of proteins was analyzed by western blotting. The original blots are shown in Supplementary Fig. S9. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28266648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - Impaired hepatic SIRT1-FoxO signaling in L-G6pc-/- mice.(A) Western blots & densitometry analysis (n = 5), & quantification of mRNA for hepatic SIRT1 & FoxO3a (n = 8). (B) Hepatic NAD+ levels (n = 9). (C) Western blots & densitometry analysis of PPAR-gamma , PPAR-alpha & beta -actin (n = 5). (D) Immunohistochemical analysis of hepatic ChREBP & quantification of nuclear ChREBP-translocated cells (n = 4). Scale bar, 25 μm. (E) Quantification of mRNA for hepatic Acaca, Fasn & Elovl6 by real-time RT-PCR (n = 6). (F) Western blots of acetylated & total FoxO3a after immunoprecipitation of nuclear extracts using anti-FoxO3a, & quantification of the acetylated FoxO3a/total FoxO3a (n = 5). Data represent the mean ± SEM. *P < 0.05, **P < 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28558013), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Expressing recombinant ChREBP beta in Rictor-deficient adipocytes rescues expression of DNL enzymes.Western blot of indicated proteins in differentiated adipocytes with or without Rictor deletion transfected with various rescue constructs that were stably expressed in cells before differentiation. ‘*' indicates ChREBP beta based on molecular weight. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Hepatic expression of mRNAs encoding carbohydrate response element-binding protein (ChREBP) (a), liver pyruvate kinase (LPK) (c), & microsomal triglyceride transfer protein (MTTP) (d), & nuclear ChREBP protein (b) in water-control, 10% fructose solution-control, & 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 & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23737835), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR mediate the induction of lipogenesis induced by an oleic acid-rich diet.(A) Hepatic Acly, Acaca, Acacb, Fasn, Elovl6, Scd1 mRNA levels quantified by qPCR. (B) Cytoplasmic protein expression levels of P-ACLY, ACLY, ACC, ELOVL6, SCD1, FASN & beta -ACTIN assayed by Western Blotting. (C) Fads1, Fads2, Elovl5, Gpat, Pnpla3 & Lpk mRNA quantification assayed by qPCR. (D) Srebp-1c & Chrebp mRNA quantification assayed by qPCR. (E) Cytoplasmic & nuclear expression levels of LXR, SREBP-1c & ChREBP assayed by Western Blotting. Data are the mean±SEM of values measured in LXR+/+ & LXR-/- mice fed REF or OLIV diet. a Significant genotype effect. b Significant difference versus REF diet (n = 6 mice per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28732092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Analysis of protein levels in livers transfected with GK & GKA456V. Livers excised from mice in postabsorptive state were homogenized & 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. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22194744), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - ChREBP knockdown inhibited glycolysis, lipogenesis & p21 in HT29 cells. (A) Inhibited relative mRNA expression of ChREBP alpha & ChREBP beta normalized to B2M after control or ChREBP siRNA transfection for 48 hours. (B) Western-blot of ChREBP, phospho-p53 & p21 & their quantification on the right. beta -actin was served as a loading control. Proteins were extracted from cells transfected with sicontrol & siChREBP after 48 hours. The quantification of western blot was normalized to beta -actin. (C) Decreased relative mRNA expression of glycolytic & lipogenic genes, normalized to B2M. (D) Relative mRNA expression of p53 & p21, normalized to B2M. (E) Relative mRNA expression of cell Cyclins, normalized to B2M. n = 4. *p < 0.05; **p < 0.01; ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32144313), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Ligand-activated LXR reduces ChREBP binding to chromatin. (A). Left panels: Local pattern of LXR-ChREBP co-occupancy. Browser view of LXR & ChREBP tracks in the promoter region of Lpk (Pklr), Txnip, Fasn & Scd1. Square brackets indicate the scale maxima of ChIP/input ratios. Arrows indicate the genomic locations of quantitative RT-PCR primers. Right panel: AML12 cells transfected with ChREBP alpha /Mlx gamma & LXR alpha /RXR alpha were treated with DMSO (0.1%) or GW3965 (10 µM) for 18 h. ChREBP or LXR binding to genomic location indicated in the right panels were detected by ChIP using antibodies against ChREBP, LXR or IgG as negative control. Data are presented as mean ± SEM (n = 3–5). Significant differences are shown as * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ChIP-IgG & #p < 0.05, ##p < 0.01, ###p < 0.001 between DMSO & GW3965 groups. ns, not significant. (B). CoIP of LXR alpha & ChREBP alpha , expressed in COS-1 cells cultured in 25 mM glucose, treated with DMSO (0.1%) or GW3965 (1 µM) for 18 h. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or LXR alpha antibodies. One representative western blot is shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Induction of hepatic Srebp-1 & carbohydrate response element-binding protein (Chrebp) beta expression by dietary glucose is reduced in LXR alpha −/− mice. (A) Hepatic gene expression of Lxr alpha / beta , Srebp-1, & Chrebp alpha / beta was analyzed by quantitative RT-PCR & normalized to Tbp; (B) Cytosolic & nuclear lysates were immunoblotted with antibodies against LXR, SREBP-1, & ChREBP with alpha -Tubulin & Lamin A as loading controls. Each lane represents independent mice from each group. One representative western blot is shown (n = 3). Data represent the mean ± SEM (n = 5). Significant differences were found using two-way ANOVA followed by Tukey’s multiple comparison test (fasted vs. fructose fed & fasted vs. glucose fed RNA data were analyzed separately). * p < 0.05, ** p < 0.01, *** p < 0.001 compared to fasted. #p < 0.05, ##p < 0.01, ###p < 0.001 compared to LXR alpha +/+ mice. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/7/678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Decreased glucose uptake & Chrebp beta -driven DNL is a primary consequence of Rictor loss in adipocytes.(a) Western blots of indicated proteins at different days of differentiation using Rictor iKO primary adipocytes (described in Methods). (b) Oil Red O staining of differentiated adipocytes. (c) The relative mRNA level of ChREBP beta in differentiated cells at various time points. n=3. (d) 2-DG uptake in differentiated adipocytes without or with insulin stimulation. n=3. (e) The C14-glucose-derived FA in differentiated adipocytes. n=3. (f) The C14-glucose derived triglyceride (TAG) in differentiated adipocytes. n=3. (g) Relative glut4 expression in differentiated cells at various time points. n=3. (h) Relative glut4 expression in sWAT. n=8. (i) Glycerol release in differentiated adipocytes under basal & isoproterenol (Iso) stimulation. n=4. (j) Glycerol release in ex vivo pgWAT under basal & isoproterenol stimulation. n=6. Data were analysed by Student's t-test. Values are expressed as mean+s.e.m. *P<0.05; **P<0.01; ***P<0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - RetSat controls ChREBP activity & glucose sensing in primary hepatocytes. Primary mouse hepatocytes were treated with Control or RetSat siRNA for 48 h, (a, left) ChREBP mRNA expression determined by qPCR, & RetSat & ChREBP protein levels determined by immunoblotting (a, right). left, Data are shown as mean ± 11s.d., n = 3 independent transfections of hepatocyte cultures from the same mouse. Two independent experiments yielded similar results. b Hepatocytes were treated as described in a & mRNA expression of a selection of known ChREBP target genes visualized in a heatmap. c Primary hepatocytes were depleted of RetSat using two siRNA’s targeting different sites of the RetSat transcript for 48 h, & expression of the indicated genes analyzed by qPCR. Data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two different mice; *P < 0.05 between siControl und siRetSat by one-way ANOVA with Bonferroni post test. An independent experiment yielded similar results. d Hepatocytes treated with Control or RetSat siRNA were transfected with a ChoRE-Luc reporter, exposed to low & high glucose concentrations as indicated, & analyzed for luciferase activity. e Hepatocytes treated with Control or RetSat siRNA were exposed to low & high glucose concentrations as indicated, & mRNA expression determined by qPCR. In d, e, data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two mice; two-way ANOVA with Bonferroni post test revealed significances between low & high glucose concentrations (#P < 0.05) & between siControl & siRetSat (*P < 0.05). An independent experiment yielded similar results Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR alpha & ChREBP alpha interact via key activation domains. (A). Top panel: Schematic representation of the ChREBP alpha full-length (FL), ChREBP beta & the low glucose inhibitory domain (LID) protein. Bottom panel: CoIP of LXR alpha & ChREBP alpha , ChREBP beta or LID, expressed in COS-1 cells cultured in 25 mM glucose. The ChREBP expression plasmids were transfected with a DNA ratio of ChREBP alpha :ChREBP beta :LID = 1:6:1, to obtain comparable protein levels. Lysates were immunoprecipitated with ChREBP, FLAG (for LID) or LXR alpha antibodies & input & immunoprecipitated proteins immunoblotted with the same antibodies (n = 3). One representative western blot is shown. LID, low-glucose inhibitory domain; GRACE, glucose-response activation conserved element; bHLH, basic helix-loop-helix domain: ZIP, leucine zipper. (B). Top panel: Schematic representation of the LXR alpha FL & truncations. Bottom panel: CoIP of ChREBP alpha & LXR alpha FL or truncations expressed in COS-1 cells cultured in 25 mM glucose. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or FLAG (for LXR alpha FL & truncations) antibodies. One representative western blot is shown. NTD, N-terminal domain; DBD, DNA-binding domain; LBD, ligand-binding domain. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - FXR inhibits glucose-induced proglucagon expression(a) Proglucagon qPCR on cDNA from GLUTag cells starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate (10 mmol L−1), glucose (5.6 mmol L−1) or 2-deoxyglucose (5.6 mmol L−1) media containing DMSO, GW4064 (5 μmol L−1) or CDCA (100 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. ***P≤0.001: effect of GW4064 & CDCA on proglucagon mRNA levels in each medium conditions. §§§P≤0.001: effect of glucose on proglucagon mRNA levels in DMSO, GW4064 & CDCA conditions. (b) Chrebp qPCR on cDNA from FACS-sorted proglucagon-negative & proglucagon-positive cells from the ileum (ileum L−; ileum L+) & colon (colon L−; colon L+) of GLU-VENUS mice (lower panel; n=3) & ChREBP protein expression from cytoplasm & nucleus extract from GLUTag cells (upper panel; performed 3 times). Data are represented as mean +/− SD. Student t-test. *P≤0.05 & **P≤0.01 (c) ChREBP & FXR western-blots after FXR immunoprecipitation on lysates from cytoplasm & nucleus of GLUTag cells treated or not with GW4064 (5 μmol L-1) in presence or not of glucose (5.6 mmol L−1) (performed 2 times). (d) Proglucagon qPCR on cDNA from GLUTag cells electroporated with a siCtrl or siChrebp, starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate 10 mmol L−1 (Glc −) or glucose 5.6 mmol L−1 (Glc +) media supplemented with DMSO or GW4064 (5 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. *P≤0.05 & **P≤0.01: effect of treatments on each transfection condition. §§§P≤0.001: effect of siChrebp in each treatment condition. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms8629), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Phf2 expression is increased in the liver of obese patients with benign hepatic steatosis & positively correlates with insulin sensitivity. Human liver biopsies from lean subjects with no fatty liver (NoFL) or obese patients with simple steatosis or NASH were obtained from the ABOS cohort. a Representative Western blot analysis of Phf2, ChREBP, SCD1, Nrf2, Gpx4, & alpha -SMA expression (n = 10 per group). b ChIP experiments for H3K9me2 levels & for the recruitment of ChREBP & the RNA polII at the SCD1 & Nrf2 promoter (n = 10 per group). c MUFA/SFA ratio reflecting SCD1 activity (n = 10 per group). d Expression of Nrf2 & Nrf2-regulated genes (n = 10 per group). e Levels of carbonylated proteins (n = 10 per group). f Expression of coll-Ia1, alpha -SMA, & TIMP-1 (n = 10 per group). All error bars represent mean ± SEM. Statistical analyses were made using Anova, followed by Bonferonni’s test. *Obese with steatosis compared to lean with noFL; P < 0.01. **Obese with steatosis compared to obese with NASH; P < 0.05 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-04361-y), 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
CoraFluor 1	NB400-135CL1
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 525	NB400-135JF525
Janelia Fluor 549	NB400-135JF549
Janelia Fluor 646	NB400-135JF646
Janelia Fluor 669	NB400-135JF669
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

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NB300-605

iNOS Antibody - BSA Free

(3 Reviews)

(141 Publications)

200uL

NB300-605

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

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

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

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

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

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Stimulation of IMA 2.1 cells had no effect on relative survival after viral infection. IMA 2.1 cells were stimulated with LPS (10 µg/ml), IFN-gamma , (10 ng/ml) LPS + IFN-gamma , IL-4 (10 ng/ml), FGF (5 ng/ml) or FGF + LPS for 24 h in medium with 2% FBS. Polarization of cells was analyzed by Griess assay (a), Western blot (b) & FACS analysis by detection of MHCII+ cells (c). d MTT assay was performed to detect the relative percentage of VACV-mediated cell death in the presence of stimulating factors. e Viral replication was analyzed by standard plaque assay in the presence of stimulating factors. All experiments were performed in triplicate. Image collected & cropped by CiteAb from the following publication (//www.translational-medicine.com/content/13/1/216), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: iNOS Antibody - BSA Free [NB300-605] - Nfix is mainly expressed by anti-inflammatory MPs. (a) Percentage of F4/80+ MPs positive for Nfix in Tibialis Anterior muscles (TA) of WT mice injected by CTX at D2, D4 & D7, post-injury. Immunostaining for F4/80 (green), Nfix (red) & DAPI (blue) at D4 & D7 after CTX injection; (b) Percentage of Ly6C+ & Ly6C- sorted MPs positive for Nfix in TA muscles of WT mice injected by CTX at D2, D4 & D7 post-injury; (c) Percentage of Nfix+ MPs after M1 & M2c polarization (with IFN gamma & IL10, respectively). * p < 0.05; *** p < 0.001; for (b) * p < 0.05 Ly6C+ vs. Ly6C+ at D4 & D7; # p < 0.05 Ly6C− D7 vs. D2. Results are means ± SEM of at least three independent experiments. Scale bar = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183151), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Indolepropionic acid (IPA) induced oxidative stress, cellular energy stress, & decreased the proportions of cancer stem cells. 500,000 cells/well 4T1 cells were treated with IPA in the concentrations indicated for 24 h; then, (A) lipid peroxidation was measured by TBARS assay, & (B) 4HNE expression was assessed by Western blotting (representative figure, n = 3). In the same cells (C), the protein expression of NRF2 (at 68 kDa) & iNOS were determined by Western blotting (n = 3), while (D) the mRNA expression of catalase (cat) was determined by RT-qPCR (n = 3). (E) The expression of the indicated proteins (pACC, ACC, FOXO1, & PGC-1 beta ) were determined by Western blotting (n = 3, except for PGC-1 beta , where n = 2). (F) 100,000 cells/well 4T1 cells were treated with the indicated concentration of IPA for 24 h; then, the proportions of aldehyde dehydrogenase-positive cells were determined in Aldefluor assays using flow cytometry (n = 3). For Western blots, a typical experiment was displayed. Fold data were log2 transformed to achieve normal distribution. Statistical significance was determined using the ANOVA test followed by Dunnett’s post-hoc test, except for panel F, where Student’s t-test was used. * & *** indicate statistically significant difference between control & treated samples at p < 0.05 & p < 0.001, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32854297), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - NRF2 activation modulated LCA-induced oxidative stress responses in 4T1 breast cancer cells. The 4T1 cells were treated with 0.3 μm LCA & the NRF2 activator RA839 or tBHQ in the concentrations indicated for 48 h. Lipid peroxidation was determined by measuring (A) TBARS (n = 4) & (B,C) 4-HNE levels using western blotting (n = 3). (D) The 4T1 cells were treated with LCA (0.3 μm) and/or GSH & NAC (both at 5 mm) antioxidants for 48 h, then total protein concentration was determined using the sulforhodamine B assay (n = 3). For statistical analysis ANOVA test was used followed by the Dunnett post-hoc test, where all groups were compared to the LCA-treated cohort. Data are plotted as mean ± SEM. ** p < 0.01, LCA vs. LCA/NRF2-activator-treated groups (GSH, reduced glutathione; LCA, lithocholic acid; NAC, N-acetylcysteine; TBARS, thiobarbituric acid reactive substances; 4HNE, 4-hydroxynonenal). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31461945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Impaired amount of virus progeny after stimulation of BV-2 cells with IFN-gamma or IFN-gamma & LPS. BV-2 cells were stimulated with LPS (10 µg/ml), IFN-gamma , (10 ng/ml), LPS + IFN-gamma or IL-4 (10 ng/ml) for 24 h in medium with 2% FBS. Polarization of cells was analyzed by Griess assay (a), Western blot (b) & by detection of the percentage of MHCII+ cells by FACS analysis (c). The amount of virus progeny (pfu/ml) was analyzed by standard plaque assay in the presence of stimulating factors & in normal growth medium in cells & supernatants (d). Statistical analysis was performed related to infection medium. To analyze the recovery of viral replication, normal growth medium was applied after infection of pre-stimulated cells. Standard plaque assay was performed to determine viral progeny in cells & supernatant after 24, 48, 72 & 96 hpi (e). To analyze the relative survival of the cells in the presence of stimulating factors a MTT assay was performed (f). The cellular density of stimulated cells relative to unstimulated (w/o) cells was detected via optical density measurement after 24 & 48 h of cultivation (g). Two-sided t test with unequal variances was used for statistics *p < 0.05, **p < 0.01, ***p < 0.001. Active replication was defined as virus titer above the virus titer of the infection medium (red line). All experiments were performed in triplicate & repeated in an independent experiment. Image collected & cropped by CiteAb from the following publication (//www.translational-medicine.com/content/13/1/216), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Inhibitory effect of MMPP on amyloidogenesis & STAT3 translocation in astrocytes & microglia cells. The expression of APP, BACE1 & C99 was detected by Western blotting using specific antibodies in astrocytes (a) & microglia cells (b). Each blot is representative of three experiments. The activity of beta -secretase was investigated using assay kit in astrocytes (c) & microglia cells (d). Values are presented as mean ± S.D. of the three independent experiments performed in triplicate. #p < 0.05 compared to control, *p < 0.05 compared to LPS. Iba-1, COX-2, & iNOS proteins were detected by Western blotting using specific antibodies in astrocytes (e) & microglia cells (f). NO level was measured in astrocytes (g) & microglia cells (h). Activation of STAT3 was investigated using EMSA in astrocytes (i) microglial cells (j) were determined & the expression of STAT3 & phopho-STAT3 was also detected by Western blotting using specific antibodies (k), (l). For the cropped images, samples were run in the same gels under same experimental conditions & processed in parallel. Each band is representative for three experiments Image collected & cropped by CiteAb from the following publication (//link.springer.com/10.1007/s12017-017-8469-3), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-605SS

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NB400-144

CD36 Antibody - BSA Free

(9 Reviews)

(136 Publications)

0.1 ml

NB400-144

$Immunohistochemistry: CD36 Antibody [NB400-144] - Timp4-deficiency results in defective lipid digestion and absorption. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed and HFD-fed WT and Timp4-/- mice. Western blot (C) and mRNA (D) for CD36 in enterocyte fraction of chow-fed and HFD-fed WT and Timp4-/- mice (collected from the proximal small intestine). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license.$

Immunohistochemistry-Paraffin: CD36 Antibody [NB400-144] - Staining of CD36 in human adipocytes.

Western Blot: CD36 Antibody [NB400-144] - Mouse primary muscle cell lysate. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: CD36 Antibody [NB400-144] - Bone marrrow derived mouse macrophages stained with CD36 antibody. ICC/IF image submitted by a verified customer review.

Western Blot: CD36 Antibody [NB400-144] - Detection of CD36 in human adipocyte extract (30 ug). Lane 1: 0.5 ug/ml NB 400-144; lane 2: 2 ug/ml NB 400-144. ECL: 3 second exposure.

ATM activation by chloroquine alleviates senescence.(a) Immunoblots showing protein levels of ATM, NBS1, and RAP80 in human skin fibroblasts (HSFs). A gradually increased level of p16 indicates cellular senescence, while elevated gamma H2AX level indicates accumulated DNA damage. (b) Immunoblots showing protein levels of ATM, NBS1, and RAP80 in mouse embryonic fibroblasts (MEFs). (c) Immunoblots showing protein levels of ATM, NBS1, and RAP80 in brain tissues isolated from 3-, 10-, and 18-month-old male mice. (d) SA-beta -Gal staining in HSFs treated with sh-ATM or scramble shRNA. Scale bar, 100 µm. (e) Quantification of SA-beta -Gal-positive staining of (d) from five views randomly captured for each group. Data represent means ± SEM. ***p<0.001. (f) Immunoblots showing increased gamma H2AX and unaffected LC3I/II in HSFs treated with sh-ATM or scramble shRNA. (g) Immunoblots showing protein levels of pS1981 ATM, gamma H2AX, and cleaved caspase-3 in HSFs treated with 10 μM of CQ for indicated time. (h) SA-beta -Gal staining in HSFs expressing either scramble or ATM shRNA treated with 1 μM CQ or DMSO (12 hr). Scale bar, 100 µm. (i) Quantification of SA-beta -Gal-positive staining of (h) from five views randomly captured for each group. Data represent means ± SEM. ***p<0.001; ‘N.S.’ indicates no significant difference. (j) HSFs at passage 20 were continuously cultured with 1 μM CQ or DMSO, and cell number was calculated at each passage. Data represent means ± SEM. ***p<0.01. (k) Immunoblots showing protein levels of gamma H2AX, p62, and LC3 in MEFs treated with 1 μM CQ or DMSO. Note that CQ had little effect on the expression levels of p62 and LC3. (l) MEFs at passage one were continuously cultured in 20% O2 with 1 μM CQ or DMSO, and cell number was determined at each passage. Data represent means ± SEM. ***p<0.01.10.7554/eLife.34836.006Figure 1—source data 1.Statistical analysis for SA-beta -Gal positive staining.10.7554/eLife.34836.007Figure 1—source data 2.Statistical analysis for EdU positive staining.Statistical analysis for SA-beta -Gal positive staining.Statistical analysis for EdU positive staining.Decline of ATM-centered DNA repair machinery during senescence.(a) Real-time PCR analysis showing progressively elevated mRNA level of p21 in continuously cultured human endothelial cells (HUVEC). **p<0.01. (b) SA-beta -Gal staining of HUVEC cells at indicated passages. Scale bar, 100 µm. (c) HUVEC cells at P21, P18, P12, and P7 were subjected to transcriptome analysis. A minimum average rpkm value of 1.0 and maximum 10% fluctuation in young cells (P7 Vs P12) was set as the threshold. Genes were downregulated by more than 20% in pre-senescent, and senescent cells compared with young cells (P21/P18 Vs P12/P7) were selected. (d) Pathway analysis of genes identified in (c) by STRING v10. (e) Downregulation of ATM-related DNA repair genes during senescence.ATM regulates replicative senescence.(a) Representative images showing cells treated with Scramble (sh-NC) or sh-ATM. (b) Percent EdU-positive cells in sh-NC or sh-ATM treated HSFs. Views were randomly captured and at least 100 cells were included in each group. Data represent means ± SEM. ***p<0.001. (c) Immunoblots showing protein levels of pS1981 ATM and gamma H2AX in HSFs treated with 10 μM chloroquine (CQ) or 0.4 μM CPT (4 hr). Note that CQ activated ATM (pS1981) without increasing gamma H2AX, while CPT activated ATM accompanied by increased gamma H2AX. (d) SA-beta -Gal staining in primary MEFs treated with 1 μM CQ or DMSO. Scale bar, 100 µm. (e) Quantification of SA-beta -Gal-positive staining of (d) from five views randomly captured for each group. Data represent means ± SEM. ***p<0.001. (f) Percent EdU-positive cells in HSFs treated with DMSO, 1 μM or 10 μM CQ. Views were randomly captured and at least 100 cells were included in each group. Data represent means ± SEM. ***p<0.001. (g) Representative images showing proliferative HSFs treated with different doses of CQ for the indicated time points. (h) Immunoblots showing LC3B levels in HSFs treated with indicated dose of CQ for indicated period of time. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29717979), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Rabbit Polyclonal CD36 Antibody [NB400-144] - The western blot was conducted on avian (passerine) skeletal muscle tissue homogenate. 6ug of total protein was loaded and GAPDH was probed to ensure total protein loads were similar across samples. Rabbit polyclonal CD36 antibody (NB400-144) was used at 1:5000 dilution (diluted in 5% milk). CD36 and GAPDH were probed sequentially - not multiplexed. CD36 produced a band above 40kDa and GAPDH at 36kDa. Image from a verified customer review.

$Immunocytochemistry/ Immunofluorescence: CD36 Antibody - BSA Free [NB400-144] - Timp4-deficiency results in defective lipid digestion & absorption. Fecal triglyceride (TG) content (Ai) in chow- or HFD-fed WT & Timp4−/− mice. Fecal lipid analysis by thin layer chromatography in chow-fed (Aii) & HFD-fed (iii) WT & Timp4−/− mice. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed & HFD-fed WT & Timp4−/− mice. Western blot (C) & mRNA (D) levels for CD36 in enterocyte fraction of chow-fed & HFD-fed WT & Timp4−/− mice (collected from the proximal small intestine). (E) Triglyceride levels in enterocytes collected from the proximal small intestine. Averaged data are presented as mean ± S.E.M & analyzed by ANOVA. * indicates significance (p < 0.05). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: CD36 Antibody - BSA Free [NB400-144] - Timp4-deficiency results in defective lipid digestion & absorption. Fecal triglyceride (TG) content (Ai) in chow- or HFD-fed WT & Timp4−/− mice. Fecal lipid analysis by thin layer chromatography in chow-fed (Aii) & HFD-fed (iii) WT & Timp4−/− mice. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed & HFD-fed WT & Timp4−/− mice. Western blot (C) & mRNA (D) levels for CD36 in enterocyte fraction of chow-fed & HFD-fed WT & Timp4−/− mice (collected from the proximal small intestine). (E) Triglyceride levels in enterocytes collected from the proximal small intestine. Averaged data are presented as mean ± S.E.M & analyzed by ANOVA. * indicates significance (p < 0.05). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: CD36 Antibody - BSA Free [NB400-144] - MiR-29a inhibits the expression of fatty acid translocase CD36 by targeting 3’ untranslated region (UTR). (A) qPCR analysis of Cd36 in live tissue. (B) Representative immunoblotting bands & densitometric results of CD36 in liver tissue. (C) qPCR analysis of cd36 expression of HepG2 cells in vitro after 48h transfection of scramble sequence or miR-29a-mimic. Data obtained from six independent experiments. (D) Upper panel, sequence information, & mutual pairing status of CD36-3’UTR, mmu-miR29a, & CD36-3’UTR Mut. Note that red characters represent mismatching sites. HepG2 was first transfected with CD36-3’UTR or CD36-3’UTR mutant luciferase reporter construct then treated with control medium (ctrl), miRNA-scramble, or miR-29a mimic, & finally lysed to detect the luciferase signal. Data are expressed as mean ± SE. * p < 0.05, ** p < 0.01, & *** p < 0.001 between the indicated groups. WT, wild type mice. HFD, high-fat diet. miR-29a, mice harboring overexpression of miR-29a. mmu-miR29a, mouse-origin miR-29a. ctrl, control. Mut, mutant. UTR, untranslated region. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31652636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: CD36 Antibody - BSA Free [NB400-144] - Integrin beta 3 modulates SMC transdifferentiation. a–c Mice were fed a HFD for 6 or 16 weeks as indicated, & then transverse aortic root sections were stained. In a, b sections from ApoE(−/−), SMMHC-CreERT2, ROSA26R(mTmG/+) mice were stained for SMA, GFP (fate marker), nuclei (DAPI), & either integrin beta 3 (a) or CD36 (b). Dashed yellow lines separate cap from core (a, b) & core from media (b). n = 5. In c sections from ApoE(−/−) mice that were also wild type or null for Itgb3 were stained for SMMHC, CD68, & nuclei (DAPI). n = 3. Boxed regions (a, c) are shown as close-ups on right; in c CD68+SMMHC+ cells in the media (arrowheads) & plaque (arrows) of the Itgb3 null atherosclerotic aorta are indicated. Med, tunica media; Lu, lumen; Pl, plaque. Scale bars, 25 μm. d–h Aortic SMCs were isolated from ApoE(−/−) mice & then subjected to siRNA-mediated knockdown with si-Itgb3 vs. scrambled (Scr; d–f) or with si-Itgb3, si-Tlr4 vs. si-Itgb3 (g, h). Levels of indicated transcripts from qRT-PCR are relative to Gapdh & normalized to either Scr in d, f or to si-Itgb3 in g, h. For d, g, n = 4–5 in duplicate. In e silenced SMCs were cultured with DiI-conjugated ox-LDL for 10 h & stained with DAPI; n = 5. In f, h silenced SMCs were exposed to soluble cholesterol:methyl-beta -cyclodextrin complexes for 3 days, & then mRNA levels were assessed; n = 4–7 in duplicate. *, **, ***, ^, **** vs. control (Scr in d, f & si-Itgb3 in g, h), p < 0.05, p < 0.01, p < 0.005, p < 0.001, & p < 0.0005, respectively. NS, not significant. Student’s t-test was used, & error bars represent standard deviations. i Schematic of the effect of beta 3 reduction via TLR4 & CD36 in SMCs on transdifferentiation Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-04447-7), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CD36 Antibody - BSA Free [NB400-144] - The increase in CD36 levels caused by lipids in Sirt3-deficient hepatocytes is mediated by Nrf2. VLDLR mRNA abundance (a) & protein levels of VLDLR & NQO1, an Nrf-2-target gene, (b) were assessed in Huh-7 cells incubated with fatty acid free-BSA or BSA-palmitate (0.3 mM) & exposed to either vehicle or the Sirt3 inhibitor AAPBO (100 μM) for 16 h. a, p < 0.05 vs. CT. b, p < 0.05 vs. CT cells incubated with palmitate. c, p < 0.05 vs. CT cells treated with AAPBO. c, fatty acid uptake in Huh-7 cells incubated with fatty acid free-BSA or BSA-palmitate (0.3 mM) & exposed to either vehicle or the Sirt3 inhibitor AAPBO (100 μM) for 16 h was measured by the uptake of BODIPY-C16. a, p < 0.05 vs. CT. b, p < 0.05 vs. CT cells incubated with palmitate. c, p < 0.05 vs. CT cells treated with AAPBO. mRNA abundance (d) & protein levels of VLDLR (e) in Huh-7 cells transfected with control (CT) or SIRT3 siRNA & incubated in the presence or absence 0.3 mM palmitate (Pal) for 24 h. Protein levels of CD36 (f), NQO1 (g) & PPAR gamma (h) in Huh-7 cells transfected with control (CT) or SIRT3 siRNA & incubated in the presence or absence 0.3 mM palmitate (Pal) or the Nrf2 inhibitor ML385 (10 μM) for 24 h. a, p < 0.05 vs. CT siRNA cells. b, p < 0.05 vs. CT siRNA cells incubated with palmitate. c, p < 0.05 vs. SIRT3 siRNA cells. d, p < 0.05 vs. CT siRNA cells incubated with palmitate & ML385 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32912335), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Av, Bv, Pm, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Av, Bv, Pm, 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	NB400-144AF350
Alexa Fluor 405	NB400-144AF405
Alexa Fluor 488	NB400-144AF488
Alexa Fluor 532	NB400-144AF532
Alexa Fluor 594	NB400-144AF594
Alexa Fluor 647	NB400-144AF647
Alexa Fluor 700	NB400-144AF700
Alexa Fluor 750	NB400-144AF750
Allophycocyanin	NB400-144APC
Biotin	NB400-144B
CoraFluor 1	NB400-144CL1
DyLight 350	NB400-144UV
DyLight 405	NB400-144V
DyLight 488	NB400-144G
DyLight 550	NB400-144R
DyLight 594	NB400-144DL594
DyLight 650	NB400-144C
DyLight 680	NB400-144FR
DyLight 755	NB400-144IR
FITC	NB400-144F
HRP	NB400-144H
Janelia Fluor 525	NB400-144JF525
Janelia Fluor 549	NB400-144JF549
Janelia Fluor 646	NB400-144JF646
Janelia Fluor 669	NB400-144JF669
PE	NB400-144PE
PerCP	NB400-144PCP
mFluor Violet 450 SE	NB400-144MFV450
mFluor Violet 500 SE	NB400-144MFV500
mFluor Violet 610 SE	NB400-144MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-144SS

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NB100-56875

GAPDH Antibody - BSA Free

(5 Reviews)

(128 Publications)

0.1 mg

NB100-56875

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

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

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

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

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

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB100-56875] - Overexpression of HsVps13A rescues phenotypes of Vps13 mutants.(A) Samples from fly heads of Actin-GAL4 / + (as a control) & Actin-GAL4 / UAS-HsVps13A (HsVps13A expressing) flies were separated into a membrane & cytosol fraction & analyzed by Western blot for HsVps13A levels. EGFR & GAPDH used as controls for membrane & cytosolic proteins, respectively. (B) Eclosion rate of Vps13 mutant flies a Actin-GAL4/+ (control) or Actin-GAL4/UAS-HsVp13A (HsVps13A expressing) background at 25°C. (C) Ubiquitylated proteins from samples of 1 day old fly head extracts of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ (representing homozygous mutants) & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A (representing homozygous mutants expressing human VPS13A). (D) Representative picture of ubiquitylated protein staining of the third instar larval ventral nerve cord of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. Arrows indicate accumulations of ubiquitylated positive structures. The scale bar indicates 50 μm & 12,5 μm in the enlargement. (E) Quantification of the number of puncta in third instar larval ventral nerve cord of the experiment presented in Fig 6D. (F) Life span curve of Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. All quantifications show the mean & SEM of at least three independent experiments per condition. For statistical analysis a two-tailed students T-test was used in combination with a Welch’s correction if necessary. P<0.05 is *, P<0.01 is ** & P<0.001 is ***. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB100-56875] - No dystrophin expression was detected in cardiac & skeletal muscles of Dmdmdx rats.(A) Male 7 month-old rats of line 61, wild-type littermate controls (WT) & Dmdmdx were sacrificed & biopsies from tibialis cranialis muscles (TC) & hearts (H) were harvested. Western-blot of total proteins (50 µg) was incubated with NCL-DYS2 & Manex1011C monoclonal antibodies (C-terminal & exons 10/11 epitopes, respectively). This revealed undetectable levels of the 427 kDa dystrophin band in line 61 Dmdmdx rats. Muscle from a GRMD dog (GD) was used as negative control & samples from WT rats were used as positive controls. Staining with an anti-GAPDH polyclonal antibody validated equal protein loadings. (B–E) Heart & biceps femoris muscles from the same wild-type (B & C) & Dmdmdx rats (D & E) were assessed for dystrophin expression using immunohistochemistry with Mandys110 monoclonal antibody (against exons 38–39 epitope). Compared to the subsarcolemmal expression of dystrophin in wild-type muscles, no dystrophin was detected in Dmdmdx rats except for the presence in skeletal muscle of only rare scattered revertant positive fibers (arrowheads). Immunolabelling of dystrophin (B–E) Bar = 100 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110371), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB100-56875] - ABCA1, ABCG1 & SR-BI protein expressions. a & b Hepatic protein expressions of ABCA1, ABCG1 & SR-BI were significantly decreased in COMT−/− mice at GD 18.5, compared to C57BL/6 J mice. Decreased hepatic ABCA1 expression was also observed at 10 days postpartum. ATI-5261 increased ABCA1 & ABCG1 expression in the liver at 10 days postpartum. c Placental protein expressions of ABCA1 & ABCG1 was reduced in COMT−/− mice, compared to C57BL/6 J mice. ATI-5261 treatment significantly increased ABCA1 levels in the placenta of COMT−/− mice. d Representative immunoblots of the corresponding proteins in the placenta with mouse RAW264.7 cell lysate included as positive control. Similar results were obtained when the experiment was repeated with lysates prepared from three batches of tissues. Data are presented as mean ± SEM. Groups (n = 8 in all groups) were compared using one-way ANOVA with post-hoc analysis (Tukey’s procedure). *, p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30237900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Simple Western: GAPDH Antibody [NB100-56875] - Analysis of non-canonical inflammasome pathway.A LDH cytotoxicity assay in the presence of LPS or SCGB3A2 alone, or the two together (SCGB3A2 + LPS). B LDH cytotoxicity assay in the presence of various amount of nigericin. Average ± SD from more than three independent experiments. *P < 0.01, **P < 0.0001 by Tukey’s multiple comparison. C Morphology of cells cultured in the presence of LPS or SCGB3A2 alone, SCGB3A2 + LPS, or nigericin for 3 h. For nigericin-treated group, cells were primed with LPS before addition of nigericin. Black arrow indicates ballooned cells, characteristic feature of pyroptosis. D Western blotting for the cleaved forms of CASP1 (p20), CASP4 (p20), & GSDMD (N-terminal). S: SCGB3A2, N: nigericin. Experiments were repeated more than twice & same results were obtained. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33452234), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

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

Species Glossary

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

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56875SS

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NB110-58849

Nox4 Antibody - BSA Free

(8 Reviews)

(117 Publications)

0.1 ml

NB110-58849

Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - Detection of NOX4 in HUVEC whole cell lysate. Lanes 1 and 2: serum-starved HUVEC lysate denatured at 95C for 5 minutes. Lanes 3: serum-starved HUVEC lysate denatured at room temperature for 10 minutes. Image from verified customer review.

Immunocytochemistry/Immunofluorescence: Nox4 Antibody - BSA Free [NB110-58849] - Detection of NOX4 in mouse brain showing positive staining in neurons in the cortex. Image provided by Rachel Reith.

Immunohistochemistry: Nox4 Antibody - BSA Free [NB110-58849] - Detection of NOX4 in proximal convoluted tubules of the kidney using NB110-58849 at 5 ug/mL.

Immunohistochemistry: Nox4 Antibody - BSA Free [NB110-58849] - AT1-KO mice are resistant to alcohol-induced oxidative stress. Oxidative stress was examined by immunohistochemical staining of NOX4 (D) expression was examined by immunohistochemical staining. Data are presented as means +/- SD. *, P 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24124516), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - The representative images of immunohistochemical staining (A–D; sections were counterstained with hematoxylin; original magnification, × 20), & western blot assays (E,F) showed that FLL treatment decreased Nox4 expression in tibias & uteri of OVX rats (n = 9). In addition, FLL treatment also decreased cytochrome C (Cyto-C; G) & increased Bcl-2 expression (H) in the tibias of OVX rats (n = 9). Data are presented as mean ± SD. IOD denotes integrated optical density of interested areas. #p < 0.05 with Sham group, *p < 0.05 compared with OVX group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28588482), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - Blockade of LTCC suppressed CaMKII-NF-kB pathway in DOX-treated hearts. (a) Representative immunoblots & quantitative analysis of CaMKII, phosphorylated CaMKII, & GAPDH in DOX (3 doses of DOX at 6 mg/kg body weight every third day for 1 week) or control vehicle (phosphate-buffered saline: PBS) treated-C57B/6 J mouse hearts subjected to either nifedipine (Nif, 10 mg/day/day) or saline for 9 days (n = 5). (b) Representative immunoblots & quantitative analysis of NF-kappa B, phosphorylated NF-kappa B, cleaved caspase 3, & GAPDH in each group (n = 5). The experiment was conducted 3 times. (c–g) Representative immunoblotsa & quantitative analysis of ERK, phosphorylated ERK, JNK, phosphorylated JNK, Nox4, p53, & GAPDH in each group (n = 5). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31285514), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - Diabetic atrophied muscles exhibited a state of heightened oxidative stress (HSOS). (a & b) Superoxide generation was measured in frozen muscle sections of control & diabetic using dihydroethidium-based confocal microscopic staining technique. (c & d) NADPH oxidase in a membrane fraction was assessed according to procedure involving the substrate NADPH & lucigenin chemiluminescence or the Amplex Red/horseradish peroxidase fluorescence-based assays. (e & f) Muscle NADPH oxidase-related isoforms including NOX2 & NOX4 were determined at the mRNA (e) & protein levels (f) using RT-PCR & Western blotting-based techniques. (g) Mitochondrial H2O2 generation at the steady state level & in the presence of added glutamate/malate substrates was measured using the Amplex Red/horseradish peroxidase fluorescence-based assay (g). Activities of complexes I (h) & III (i) of the electron transport chain were measured using spectrophotometric-based assay. Abbreviation: C: control; D: diabetic. Values are means ± SEM for at least 6 animals/group. ∗Significantly different from corresponding control values at P ≤ 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30510624), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - Characterization of NOX4 & PKM2 in human RCC tumors & adjacent tissue. a Mitochondrial fractions were prepared from human tumors (T) or uninvolved adjacent tissue (N). NOX4 expression was examined by western blot analysis. Prohibitin was probed as a mitochondrial marker & loading control. b Quantitation of NOX4 distribution in the mitochondrial fraction from a. The results are expressed as the means using one-way ANOVA with Tukey’s post hoc test where ± S.E.M. *p < 0.05 compared to normal (N). c Mitochondria fractions were prepared from RCC tumors & NADPH-dependent superoxide generation was examined in the presence (+) or absence (−) of ATP. The results are from eight tumors & are expressed as the means using one-way ANOVA with Tukey’s post hoc test where ±S.E.M. **p < 0.01 is compared to without (−) ATP. d PKM2 & PKM1 expression was examined by western blot analysis in lysates prepared from human tumors (T) or uninvolved adjacent tissue (N) from the same patient. Actin as loading control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29051480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - Fbs stimulated by BMM differentiate into myofibroblasts via the Cyr61/Nox4 pathway. (A) Western blotting for Fb differentiation, involving analysis of specific factors such as FSP-1, NOX2, NOX4, collagen-1, & Cyr61. The expression of these factors was normalized to that of GAPDH; (B) Cells were treated with BMM for 3 or 6 h or DPI (5 μM; NOX inhibitor) for 1 h or were co-treated with DPI & BMM. ROS production was measured using the DCF-DA assay & calculated as a percentage of the mean fluorescence intensity compared with that of the control. * p < 0.05 as compared to the control; # p < 0.05 as compared to the BMM (6 h)-treated group; (C) Cells were treated with BMM for 3 h or DPI (5 μM, NOX inhibitor) for 1 h or were co-treated with DPI & BMM. Cyr61 expression was normalized to that of GAPDH after western blotting. The values indicate intensities of protein expression with respect to that of the loading control; (D) Secretion of MMPs from BMM-treated-Fbs by using conditioned medium, followed by western blotting analysis. The expression levels were normalized to PonceauS, used as a loading control. *** p < 0.001 as compared to the control. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/19/4/1164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - DSC restores redox balance in colonic tissues. A, Colitis was induced as described in Materials & Methods & treated with or without DSC (50 mg/kg). Representative bands & densitometry analysis of Nrf2 nuclear translocation & HO‐1 expression in colonic tissues. Histone H3 & beta ‐actin were used as loading control, respectively. B, Colitis was induced as described in Materials & Methods & treated with lentiviral Nox4 shRNA or lentiviral scrambled shRNA. Representative bands & densitometry analysis of Nrf2 nuclear translocation & HO‐1 expression in colonic tissues. Histone H3 & beta ‐actin were used as loading control, respectively. BMDM was stimulated with or without DSC (50 μmol/L) as described in Materials & Methods. C, Representative bands & densitometry analysis of Nox4. beta ‐actin was used as loading control. D, Representative bands & densitometry analysis of Nrf2 nuclear translocation & cytoplasmic HO‐1 expression in BMDM. beta ‐actin or histone H3 was used as loading control. Data shown are means ± SEM of n = 8 in each group. *P < 0.05 vs Control cell or mice (CTL), #P < 0.05 vs DSS‐treated mice or LPS‐stimulated cells Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32945118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Nox4 Antibody - BSA Free [NB110-58849] - DSC ameliorates Nox4 expression & ROS production. A, Colitis was induced as described in Materials & Methods, & the colonic tissues were collected as indicated periods. Representative bands & quantitative analysis of Nox4 in colonic tissues were shown. B‐F, Colitis was induced as described in Materials & Methods & treated with or without DSC (50 mg/kg). B, Representative bands & quantitative analysis of Nox4 in colonic tissues. C, Representative images & quantitative analysis of ROS production by DHE staining in colonic tissues, scale bar = 100 μm. D, Quantitative analysis of GSH/GSSG ratio. E, Quantitative analysis of tissue H2O2 production. Colitis was induced as described in Materials & Methods & treated with or lentiviral Nox4 shRNA. F, Representative bands & quantitative analysis of Nox4 in colonic tissues. G, Representative images & quantitative analysis of colon length. H, Representative images of H&E staining & histological score. I, Representative bands & quantitative analysis of ZO‐2 & claudin‐1 expression in colonic tissues. beta ‐actin was used as loading control. Data shown are means ± SEM of n = 8 in each group. *P < 0.05 vs Control (CTL), #P < 0.05 vs DSS‐treated mice Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32945118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Pm, Rb, Sh

Species Glossary

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

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB110-58849AF350
Alexa Fluor 405	NB110-58849AF405
Alexa Fluor 488	NB110-58849AF488
Alexa Fluor 532	NB110-58849AF532
Alexa Fluor 594	NB110-58849AF594
Alexa Fluor 647	NB110-58849AF647
Alexa Fluor 700	NB110-58849AF700
Alexa Fluor 750	NB110-58849AF750
Allophycocyanin	NB110-58849APC
Biotin	NB110-58849B
CoraFluor 1	NB110-58849CL1
DyLight 350	NB110-58849UV
DyLight 405	NB110-58849V
DyLight 488	NB110-58849G
DyLight 550	NB110-58849R
DyLight 594	NB110-58849DL594
DyLight 650	NB110-58849C
DyLight 680	NB110-58849FR
DyLight 755	NB110-58849IR
FITC	NB110-58849F
HRP	NB110-58849H
Janelia Fluor 525	NB110-58849JF525
Janelia Fluor 549	NB110-58849JF549
Janelia Fluor 646	NB110-58849JF646
Janelia Fluor 669	NB110-58849JF669
PE	NB110-58849PE
PerCP	NB110-58849PCP
mFluor Violet 450 SE	NB110-58849MFV450
mFluor Violet 500 SE	NB110-58849MFV500
mFluor Violet 610 SE	NB110-58849MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-58849SS

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NB400-101

SR-BI Antibody - BSA Free

(1 Review)

(114 Publications)

0.1 ml

NB400-101

<b>Genetic Strategies Validation. </b>Immunohistochemistry: SR-BI Antibody [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 x Scarb1-KO, and Scarb1-KO mice. Liver sections from normal (b) and Tie2-Scarb1 x Scarb1-KO mice (c) were stained for SR-BI (red) and cytokeratin 8-18 (green).Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) and absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 x Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.

Western Blot: SR-BI Antibody [NB400-101] - Detection of SR-BI in mouse liver lysate (20 ug) using NB 400-101. ECL detection 5 seconds.

Flow (Intracellular): SR-BI Antibody [NB400-101] - An intracellular stain was performed on HeLa cells with NB400-101AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

$<b>Genetic Strategies Validation. </b>Western Blot: SR-BI Antibody [NB400-101] - Western blot and Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), and LIV11-SCARB1 x Scarb1-KO (lane 3) mice. 20 ug of membrane protein was loaded into each lane. (a)Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot and for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.$

Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-101] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-SR-BI at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Western Blot: SR-BI Antibody [NB400-101] - Western blot analysis of ABCA1 and SR-B1 proteins from WT and Osbpl8KO mouse liver. The blots were probed with anti-beta-actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta-actin. The data represents mean +/- s.e.m. (n=4). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license.

Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - SR-BI distribution in polarized EC SVEC4-10 cells. SR-BI localization is presented in (a) as x-y image & orthogonal (x-z & y-z) views. (b) & (c) represent rendering of SR-BI staining (red) throughout the cells. Nuclei: blue. In (b) & (c) basolateral surface is on the top & the bottom, respectively. These results demonstrate the presence of SR-BI on both the apical & the basolateral sides of EC. The size of scale bar on (a) is 5 μm & on (b) & (c) 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Western blot & Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), & LIV11-SCARB1 × Scarb1-KO (lane 3) mice. 20 μg of membrane protein was loaded into each lane. (a) Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot & for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Liver mRNA & protein expression analysis of chow-fed Osbpl8KO mice.A: qPCR analysis of the quantity of the mRNAs identified at the bottom in chow-fed KO females (open bars) & males (closed bars). The mRNAs were quantified using ribosomal protein 36B4 message as a housekeeping reference. The data are expressed relative to quantity in littermate WT animals of the same gender, & represent mean ± s.e.m. (n = 6; *p<0.05, **p<0.01, T-test). B: Western blot analysis of ABCA1 & SR-B1 proteins in WT & KO mouse liver. The blots were probed with anti-beta -actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta -actin. The data represents mean ± s.e.m. (n = 4). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Western blot & Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), & LIV11-SCARB1 × Scarb1-KO (lane 3) mice. 20 μg of membrane protein was loaded into each lane. (a) Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot & for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Bv, ChHa, Md, Pm, Sj

Species Glossary

Reactivity: Hu, Mu, Rt, Bv, ChHa, Md, Pm, Sj

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	NB400-101AF350
Alexa Fluor 405	NB400-101AF405
Alexa Fluor 488	NB400-101AF488
Alexa Fluor 532	NB400-101AF532
Alexa Fluor 594	NB400-101AF594
Alexa Fluor 647	NB400-101AF647
Alexa Fluor 700	NB400-101AF700
Alexa Fluor 750	NB400-101AF750
Allophycocyanin	NB400-101APC
Biotin	NB400-101B
CoraFluor 1	NB400-101CL1
DyLight 350	NB400-101UV
DyLight 405	NB400-101V
DyLight 488	NB400-101G
DyLight 550	NB400-101R
DyLight 594	NB400-101DL594
DyLight 650	NB400-101C
DyLight 680	NB400-101FR
DyLight 755	NB400-101IR
FITC	NB400-101F
HRP	NB400-101H
Janelia Fluor 525	NB400-101JF525
Janelia Fluor 549	NB400-101JF549
Janelia Fluor 646	NB400-101JF646
Janelia Fluor 669	NB400-101JF669
PE	NB400-101PE
PerCP	NB400-101PCP
mFluor Violet 450 SE	NB400-101MFV450
mFluor Violet 500 SE	NB400-101MFV500
mFluor Violet 610 SE	NB400-101MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-101SS

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NB600-633

IL-1 beta/IL-1F2 Antibody - Azide and BSA Free

(4 Reviews)

(115 Publications)

0.1 mg

NB600-633

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

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

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

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

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

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

Western Blot: IL-1 beta/IL-1F2 Antibody [NB600-633] - Methylene blue inhibits inflammasome formation in cultured microglia. (A) Expression of Pro-Caspase-1, Caspase-1 p20, pro-IL-1 beta & mature IL-1 beta in microglia with or without stimulation in the presence or absence of methylene blue. Left: representative Western blot images. Right: statistics. N = 5 per group. The (B) expression of NLRP3, NLRC4 & Aim2 in microglia. Left: representative Western blot images. Right: statistics. N = 4 per group. (C) Co-immunoprecipitation assay showing the binding of ASC to NLRP3 or NLRC4. Left: representative Western blot images. Right: statistics. Un: no stimulation. LPS+ATP: stimulation with LPS followed by ATP treatment. V: vehicle; M: 500 nM methylene blue. IP: immunoprecipitation with the antibody against indicated protein. IB: detection of indicated protein. To analyze the relative expression of target proteins, the band intensities of target proteins were normalized to corresponding band intensities of alpha -Tubulin, followed by calculating the expression in other groups relative to “Un (V)” group. N = 4 per group. *p < 0.05; **p < 0.01; ***p < 0.001 in comparison with unstimulated cells of the vehicle group. #p < 0.05; ##p < 0.01 in comparison with stimulated cells of the vehicle group. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fncel.2017.00391/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Rabbit Polyclonal IL-1 beta/IL-1F2 Antibody [NB600-633] - IL-1 beta/IL-1F2 Western blot of liver homogenate from control (1) and alcohol-fed mice (2). Image from a verified customer review.

Reactivity:

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

Species Glossary

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

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Validated by:

Validated by:

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NB100-355

RPE65 Antibody (401.8B11.3D9) - BSA Free

(7 Reviews)

(102 Publications)

0.2 ml

NB100-355

Immunohistochemistry-Paraffin: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Analysis of FFPE human glioblastoma tissue section using 1:500 dilution of RPE65 [401.8B11.3D9] antibody on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) with 10mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching using peroxide block. The sections were incubated with primary antibody for 30 minutes. Bond Polymer Refine Detection (Leica Biosystems) and DAB were used for signal detection which followed counterstaining with hematoxylin. Whole slide scanning and capturing of representative images (20X) were performed using Aperio AT2 (Leica Biosystems).

$Western Blot: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - WB analysis of RPE65 in 20ug lysate of COS7 cells expressing recombinant Human RPE65 (Lane 1) and 5ug of Bovine retinal pigment epithelium membrane fraction (Lane 2). Blot processed for detection with alkaline phosphatase conjugated goat-anti Mouse IgG secondary antibody and NBT/BCIP substrate.$

Immunocytochemistry/Immunofluorescence: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - ICC-IF analysis of cultured ARPE19 cells, a spontaneously arising human retinal pigment epithelia cell line - 10 minutes fixation in 4% PFA, 10 minutes permeabilization in PBS containing 0.2% Triton X-100 (PBS-T), 1 hour blocking in 10% normal goat serum containing 1% BSA in PBS-T, 1:100 primary antibody dilution in PBS, ON 4C incubation.

Immunohistochemistry-Frozen: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Staining of RPE65 in a cryosection of mouse retina tissue using RPE65 antibody (clone 401.8B11.3D9).

Immunohistochemistry: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Zebrafish brain ventricular area labeled with mouse anti-RPE65 (1:100). This image was submitted through a verified customer review.

Simple Western: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - iPSC-RPE from all donors express RPE marker proteins. iPSC-RPE from the patient, the patients mom, the patients dad, and the three unrelated, unaffected controls all expressed RPE65. The negative control (iPSCs) had no detectable RPE65 protein expression. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29540715/) licensed under a CC-BY license.

<b>Genetic Strategies Validation. </b>Western Blot: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Immunoblotting showing the expression of RPE-specific proteins BEST1 (NB300-164), RPE65 (NB100-355), CRALBP, and the loading control beta-Actin in iPSC-RPE cells. Two gels/blots in the same panel were prepared from the same cell lysate of each PSC-RPE to detect BEST1 + beta-Actin, and RPE65 + CRALBP, respectively. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021/) licensed under a CC-BY license.

Western Blot: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Expression of RPE-specific marker proteins in hPSC-RPE & iPSC-RPE cells.(a–b) Immunoblotting showing the expression of RPE-specific proteins BEST1, RPE65, CRALBP, & the loading control beta -Actin in hPSC-RPE (a) & iPSC-RPE (b) cells. Two gels/blots in the same panel were prepared from the same cell lysate of each PSC-RPE to detect BEST1 + beta -Actin, & RPE65 + CRALBP, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - BMP5 induces ectopic RPE development in the central NR at optic cup stages. (A,B) Peripheral, untreated chick eye at E8 showing pigmentation & MITF expression being restricted to the outer layer of the eye. The arrowheads indicate the peripheral NR. (C-F) Higher magnification of the central chick eye at E8 showing the pigmented RPE, where RPE65 protein is detected (arrows). Faint Wnt2b & strong Vsx2 expression is detected in the central NR. The arrows indicate the RPE. (G,H) Following BMP5 application at E3.5/4, the NR detached (arrowhead) & MITF protein is now detected in the central NR (cNR). Note that a part of the cNR has RPE-like morphology (eRPE). (I-L) Higher magnification images of the eRPE. Ectopic pigment granulae, RPE65 protein & strong Wnt2b expression are detected in this region, whereas Vsx2 expression is downregulated (arrowheads). (M-O) Untreated chick eye at E8 showing pigmentation & MITF (arrow) & VSX2 protein distribution, restricted to the RPE & NR, respectively. (P-R) Following BMP5 application at E3.5/4, ectopic pigmentation & nuclear MITF protein are detected in the inner optic cup (arrowheads), whereas VSX2 protein is only weakly or not detected. The arrows indicate the RPE. (S) Graphical representation of the average thickness of the inner layer of the untreated (control) & BMP5-treated eye at E8. All expression pattern studies included n≥5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28546339), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Pm, Xp

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Pm, Xp

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-355AF350
Alexa Fluor 405	NB100-355AF405
Alexa Fluor 488	NB100-355AF488
Alexa Fluor 532	NB100-355AF532
Alexa Fluor 594	NB100-355AF594
Alexa Fluor 647	NB100-355AF647
Alexa Fluor 700	NB100-355AF700
Alexa Fluor 750	NB100-355AF750
Allophycocyanin	NB100-355APC
Biotin	NB100-355B
DyLight 350	NB100-355UV
DyLight 405	NB100-355V
DyLight 488	NB100-355G
DyLight 550	NB100-355R
DyLight 594	NB100-355DL594
DyLight 650	NB100-355C
DyLight 680	NB100-355FR
DyLight 755	NB100-355IR
FITC	NB100-355F
HRP	NB100-355H
Janelia Fluor 525	NB100-355JF525
Janelia Fluor 549	NB100-355JF549
Janelia Fluor 646	NB100-355JF646
Janelia Fluor 669	NB100-355JF669
PE	NB100-355PE
PerCP	NB100-355PCP

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-355SS
Azide and BSA Free	NBP2-80931

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NB300-110

Tyrosine Hydroxylase Antibody - Azide Free

(5 Reviews)

(102 Publications)

0.1 ml

NB300-110

Immunocytochemistry/Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Alpha-Synuclein overexpression or intracerebral seeding impacts the dopaminergic system. Increased levels of ser129-phosphosynuclein in the substantia nigra (arrows) indicate alpha-syn stress in PFF injected animals. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30050065/) licensed under a CC-BY license.

Immunohistochemistry: Tyrosine Hydroxylase Antibody [NB300-110] - Mouse cryo-sections. Antibody at 1:500. Secondary antibody: dk-anti-sp Alexa Fluor488 at 1:500; 1 h. IHC image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Nmnat by itself does not protect dopaminergic neurons from MPP+ toxicity. Similar transduction efficiencies of the different lentiviruses were confirmed by quantifying the number of TH+ and GFP+ cells following transduction of dopaminergic cultures. Quantification of TH+ cell bodies and (E) TH+ neurites show that only WldS-transduced cultures protected neurites against MPP+. Data are normalized to control cultures and denote the mean +/- SEM of representative determinations made in three separate cultures. *p 99.8% posterior probability); green, expressed above baseline in human (>99.8% posterior probability); gray, not expressed above baseline.(F) Validation of LMO3 expression by immunohistochemistry in a subset of TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm).(G) Validation of BNC2 expression by immunohistochemistry in TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0092867416313095), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Developmental song exposure & social context affect cFOS expression in TH neurons of the caudal VTA. Sagittal drawings (A,C) & photomicrographs of tyrosine hydroxylase (TH; green label) expression (B,D) in the ventral tegmental area (VTA) & periaqueductal gray (PAG; panels A,B), & the substantia nigra pars compacta (SNc) & locus coeruleus (LC; panels C,D). (E) Examples of co-localized expression of TH (green) & cFOS (red) in the caudal VTA of a normally-reared bird that heard silence (left panel), UD song (middle panel; UD song) & FD song (FD; right panel). White arrows indicate examples of colocalized expression. (F) Percent of TH neurons co-localized with cFOS in the caudal VTA (cVTA), rostral VTA (rVTA) & SNc. Box-and-whisker plots for normally-reared (yellow colors) & song-naïve (green colors) hearing UD (UD; lighter colors) or female-directed (FD; darker colors) songs. Each box spans the interquartile range, horizontal white lines indicate the median & whiskers show the minima & maxima. Levels of cFOS expression in TH neurons for silence controls are plotted as the mean (gray dashed line) +/− standard error (gray boxes). *Indicates a significant difference at p 99.8% posterior probability); green, expressed above baseline in human (>99.8% posterior probability); gray, not expressed above baseline.(F) Validation of LMO3 expression by immunohistochemistry in a subset of TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm).(G) Validation of BNC2 expression by immunohistochemistry in TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0092867416313095), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Conversion of hNES cells into hPRogFPM & their differentiation into midbrain dopaminergic neurons. a Schematic representation of the conversion & differentiation protocols. b, cRT-qPCR analysis at day 8, showing the expression of midbrain-hindbrain TFs, such as OTX2, GBX2, LMX1A, & FOXA2 (b), as well as the dopaminergic neuron markers, NR4A2, TH, SLC18A22, & SLC6A3 (c). d Immunocytochemistry analysis of the presence of OTX2 & TH in control unconverted NES cultures, compared with NES cells converted with SAF+Dkk1 & differentiated until day 8. e, f Percentage of OTX2+ & TH+ cells in the conditions in d. P = 0.02673 (e), P = 0.03233 (f), n = 3. g–i Expression of the key midbrain TFs, LMX1A, NR4A2, & PBX1, in TH+cells derived from SAI2-NES cells after conversion & differentiation. j, k TH+ cells express the mature neuronal marker, MAP2 (j), & some acquire mature neuronal morphologies, with long processes & varicosities at day 8 (k). Scale 50μm. Box plots (b, c, e, f): Center line, median; hinges, 25% & 75% quartiles; whiskers, 1.5 interquartile range. Statistics: (b, c) ANOVA, followed by pair-wise t-test with Bonferroni correction for multiple testing. (e, f). Two sample t-test; *P ≤ 0,05; **P ≤ 0,01; ***P ≤ 0,001. N = 3 (GBX2, FOXA2, TH, SLC6A3), n = 4 (LMX1A, OTX2, NR4A2, SLC18A2) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29968757), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Comparison of Mouse & Human Dopaminergic Neuronal Development(A) WNT1 compartments marking lateral population of the floor plate in human & mouse tissue (scale bar, 100 μm).(B) Bar plot of cell types of the human & mouse dopaminergic lineage, showing the expression of key genes. Bars show average mRNA expression, scaled to the absolute molecule counts indicated on the right axis. Error bars show SEM.(C) Validation of mNbM by in situ hybridization for Igfbpl1 & Nhlh1 (scale bar, 50 μm).(D) Neuroblasts in human & mouse ventral midbrain (scale bar, 100 μm; magnification, 20 μm).(E) Selected genes showing similar (left) or distinct (right) expression in mouse & human ventral midbrain. Blue, expressed above baseline in mouse (>99.8% posterior probability); green, expressed above baseline in human (>99.8% posterior probability); gray, not expressed above baseline.(F) Validation of LMO3 expression by immunohistochemistry in a subset of TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm).(G) Validation of BNC2 expression by immunohistochemistry in TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0092867416313095), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Am, Av, Ma, Rb, Re, Ch

Species Glossary

Reactivity: Hu, Mu, Rt, Am, Av, Ma, Rb, Re, Ch

Applications:

, , , ,

Applications: , , , ,

Host:

Sheep Polyclonal

Host: Sheep Polyclonal

Alt Catalog#

IMG-5070

Alt Catalog# IMG-5070

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
Azide Free	NB300-110SS

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NB100-137

EGLN1/PHD2 Antibody - BSA Free

(12 Reviews)

(93 Publications)

0.1 mg

NB100-137

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Analysis of PHD2 expression in human prostate cancer cell lines. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-137] - Staining of endogenous PHD2 in U2OS cells. ICC/IF image submitted by a verified customer review.

<b>Genetic Strategies Validation. </b>Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Detection of PHD2 in human glioblastoma cell lysates. Image submitted by a verified customer review.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Detection of human PHD2 by Western blot. Recombinant epitope-tagged PHD1, PHD2 or PHD3 (10 ng/lane) or whole cell lysate from HeLa cells. EGLN1/PHD2 antibody used at 1 ug/mL. Detection by chemiluminescence.

Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-137] - EGLN1/PHD2 and EGFR expression levels positively correlate in breast cancer. Processed tissue microarrays of breast cancer biopsies from 313 patients were stained with EGLN1/PHD2 and EGFR antibodies. Four representative immunohistochemistries of human breast cancer with low and high expression of EGLN1/PHD2 and EGFR are shown. Magnification 10x. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/14241/text/) licensed under a CC-BY license.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Exogenous PHD2 has no impact on the gene expression of HIF-1alpha and HIF-2alpha. U87MG cells were transfected with empty vector (pcDNA) or PHD2 plasmid. Twenty-four hours after transfection, PHD2 was detected by immunoblotting. beta-Actin was used as loading control. The results are representative for three independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014295), licensed under a CC-BY license.

Flow Cytometry: EGLN1/PHD2 Antibody [NB100-137] - An intracellular stain was performed on Jurkat cells with NB100-137AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Analysis of PHD2 in normoxia (lane 1) or hypoxia (lane 2) treated SK-N-BE(2) cells using anti-EGLN1/PHD2 antibody. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-137] - Staining of PHD2 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).

Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-137] - Staining of lung vascular endothelium with EGLN1/PHD2 antibody. Image at 40X.

Flow Cytometry: EGLN1/PHD2 Antibody [NB100-137] - Detection of PHD2 in Jurkat cells. One million Jurkat cells were fixed, permeabilized, and stained with 3.0 ug/mL anti-EGLN1/PHD2 antibody in a 150 uL reaction. Isotype control (black), anti-MLL1 (red).

PHD2 and EGFR expression levels positively correlate in breast cancerProcessed tissue microarrays of breast cancer biopsies from 313 patients were stained with PHD2 and EGFR antibodies (cf Materials and methods). Four representative immunohistochemistries of human breast cancer with low and high expression of PHD2 and EGFR are shown. Magnification 10x.

Initial characterization of the OS-9 protein.(A) OS-9 expression in various human cell lines. Equal protein amounts of total cell lysates were used for SDS-PAGE & subsequent Western blotting. For each cell line, two independent samples are shown. Endogenous OS-9 was detected with a polyclonal antibody raised against a peptide corresponding to amino acids 600–667 of isoform 1 of OS-9. (B) Protein stability assay of endogenous OS-9. U2OS cells were treated with the translational inhibitor cycloheximide (100 µM). At indicated time points, whole cell lysates were analysed by immunoblotting. (C) Effect of hypoxia on OS-9 expression. For hypoxia, UT-7 cells were exposed to 1% O2 for 24 h prior to Western blot analysis. To determine any influence of HIF-1 alpha on OS-9 expression under normoxia, cells were incubated with the prolyl hydroxylase inhibitor DMOG (0.5 mM) for 24 h. (D) Protein interaction between OS-9 & PHD2 in vitro. For co-immunoprecipitation, U2OS cells were transiently co-transfected with the plasmids pOS-9-V5 & pPHD2-His, lysed in NP40 buffer, & subjected to immunoisolation with anti-V5 antibody recognizing OS-9 by its V5-tag. OS-9 & its associated proteins were separated by SDS-PAGE & analyzed by Western blot (lane 2). As controls, samples of untransfected (lane 1) cells or cells transfected with a single plasmid (lanes 3–4) were loaded. Representative Western blots are shown for each subfigure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Cellular localization of OS-9 & PHD2.(A) A lectin gel-shift assay was conducted to test for glycosylated proteins. Total cell lysates of U2OS cells were incubated in the presence or absence of the endoglycosidases EndoH & PNGaseF for 6 h at 37°C. Digest products were separated on a reducing 10% SDS-PAGE gel which contained concanavalin A co-polymerized in the top layer of the separating gel to retard mobility of glycosylated proteins [56]. Glycosylated OS-9 is indicated as ‘g’, deglycosylated OS-9 as ‘d’. (B) Detection of OS-9 & PHD2 in the nuclear fraction. HEK293 cells with & without transfection of the plasmid pcDNA3-OS-9 were separated into nuclear fraction (N) & postnuclear supernatant (PS), the latter containing cytoplasm & organelles. Western blot analysis included BiP, GAPDH & lamin A as typical marker proteins for the ER, the cytoplasm & the nucleus, respectively. (C) Detection of OS-9 & PHD2 in the cytoplasm. HEK293 cells were co-transfected with pcDNA3-OS-9 & pPHD2-V5. For hypoxia, cells were exposed to 3% O2 for 4 h. Cells were treated with 50 µg/ml digitonin & centrifuged to obtain a cytoplasmic (C) & an organelle fraction (O) & subjected to immunoblotting. (D) Isolation of cellular endomembranes. HEK293 cells were lysed mechanically by several passages through a 30½G needle. The postnuclear supernatant was processed further by ultra-centrifugation to separate the organelles (O) from the cytosol (C). High salt treatment (1 M KCl) of the organelle fraction produced a wash fraction (W) that contained dissociated peripheral membrane proteins. For immunoblot analysis of subcellular fractionations, cell aliquots were normalized for cell number prior to loading (B–D). Representative Western blots are shown for each subfigure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Representative picture of western blot in histopathologically unchanged tissue (N) & primary cancerous tissue (C) from patients with CRC. Immunodetection of bands was performed with Rp anti- PHD1, - PHD2, - PHD3 & - FIH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. The membrane was stripped & incubated with Rp anti-GAPDH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. Bands were revealed using SuperSignal West Femto Chemiluminescent Substrate, Thermo Fisher Scientific (Rockford, IL) & Biospectrum® Imaging System 500, UVP Ltd. (Upland, CA). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24195777), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - OS-9 shows no effect on regulation of HIF-1 alpha .Total cell lysates were used for SDS-PAGE & subsequent Western blotting. To generate nearly anoxic conditions, cells were exposed to an oxygen consuming chemical system or to 1% or 3% O2 for 4 h to generate hypoxia. (A) U2OS, HeLa & Hep3B cells were transiently transfected with the plasmid pOS-9-V5 48 h prior to the experiment. Lamin A & actin were used as loading controls. (B) U2OS cells were subjected to ER stress by incubation either with tunicamycin (1 µg/ml) or thapsigargin (0.5 µg/ml) for 20 h. To detect HIF-1 alpha under normoxia, cells were treated with DMOG (1 mM) for 4 h. A sample of DMSO-only treated cells was loaded to exclude unspecific side effects of the solvent. (C) U2OS cells were transduced with lentiviral construct pLKO.1-shRNA-OS-9 (shOS-9) mediating a stable knockdown of OS-9 expression. Control cells (c) were transduced with plasmid pLKO.1-puro. Representative Western blots are shown for each subfigure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Oxygen chemotaxis is independent of the PHD/HIF pathway. a–dHIF1A, HIF2A, HIF1A+HIF2A & PHD2 CRISPR/Cas9 KO clones characterisation, respectively, regarding O2-directed migration. Left panels: immunoblot validation of HIF1A, HIF2A, HIF1A+HIF2A & PHD2 KO clones. To blot HIFs factors (a, b, c), cells were first pre-treated for 5 h with CoCl2 300 µM before protein extraction, a condition that promotes HIF factors accumulation (cf. Supplementary Fig. 8f). Middle panels: cell trajectories under confinement. Red dashed lines indicate the border of the cell cluster at 0 h. Right panels: relative distribution of MCF10A KO clones versus wt cells at the edge of the cluster at 48 h. These experiments demonstrate that HIF factors deletion does not prevent aerotaxis. e, f Tracks & redistribution of wt & PHD2 KO clone silenced for PHD3 (siPHD3) or not (siCTR). g Tracks & redistribution of MCF10A cells treated with DMOG (50 µM) or CoCl2 (50 µM) to inhibit PHDs, or with vehicle only (DMSO). These experiments demonstrate that PHDs do not participate in O2-sensing during aerotaxis. Confinement was applied for 48 h (a–g). Scale bars, 500 µm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30382089), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - PHD3 expression correlates with a mesenchymal-like morphology in pancreatic ductal adenocarcinoma cell lines.NHF-1 (Fibroblast) MiaPaca2, Panc1, CAPAN1 & BxPC3 cells were harvested for RNA & protein following 24 hours exposure to normoxia (21% O2) or hypoxia (1% O2). (A) Phase-contrast images at 10× magnification were taken of MiaPaca2 (mesenchymal-like) morphology & BxPC3 cells (differentiated, epithelial morphology) under normoxic conditions. (B) PHD3 mRNA expression was determined by qRT-PCR & graphed relative to BxPC3 in normoxia. All samples were normalized to 18S rRNA & graphed as expression relative to BxPC3-Vec Normoxia (lane 1). n = 3, error bars = 1 S.D. (C) Whole cell lysate was resolved by SDS-PAGE & blotted for beta -tubulin PHD3 & PHD2. N = normoxia, H = hypoxia (1% O2). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0083021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Iron supplementation restores HIF-1 alpha levels to normal following ATP6V0E1 inhibition in HeLa cells. (A) Schematic diagram of the multimeric V-ATPase complex. (B) Chemical inhibition of V-ATPase by 10 nM BafA treatment for 24 h, increased HIF-1 alpha levels in HIF alpha -GFPODD reporter cells. Treatment with 100 μM Fe (III) citrate significantly reduced the elevated HIF-1 alpha levels associated with loss of ATP6V0E1 (1 × 106 cells per sample harvested & analyzed; N = 2). (C) Knock-down of ATP6V0E1 subunit with three different CRISPR-Cas9 guides resulted in significant upregulation of HIF-1 alpha levels in HIF alpha -GFPODD reporter cells. Co-treating cells with 100 μM Fe (III) citrate led to a reduction in HIF-1 alpha levels across the three ATP6V0E1 depleted cells. phd2 was knocked down as a control & treatment with 100 μM Fe (III) citrate did not result in reduction of HIF-1 alpha levels (1 × 106 cells per sample harvested & analyzed; N = 2). FACs plot shown is a representative image of two biological repeats performed. (D) Immunoblot analysis for HIF-1 alpha & PHD2 levels in HIF alpha -GFPODD reporter cells with either ATP6V0E1 or PHD2 depleted or treated with 10 nM BafA. The cells were treated with 100 μM Fe (III) citrate for 24 h. beta actin was used as a control. Results validated findings observed by flow cytometry, whereby HIF-1 alpha levels were upregulated following ATP6V0E1 knock-down or inhibition & levels were re-normalized upon Fe (III) citrate treatment. Treatment of Fe (III) citrate in PHD2 depleted cells did not alter HIF-1 alpha levels. All experiments were performed in biological duplicate. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32984302), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - PHD3 depletion stabilizes hypoxic p27 expression by increasing p27 half-life. a Cell cycle arrest at G0 & subsequent release shows an increase of p27 expression in siPHD3 exposed cells. b Quantification for p27 expression under PHD3 depletion at indicated time points after cell cycle release in HeLa & 786-O cells. Asterisk indicates significant difference (p < 0,05; n = 3). c Cell cycle arrest at G0 & inhibition of protein synthesis with cycloheximide indicate increased p27 stability in PHD3 depleted HeLa cells. d Quantification of p27 expression using siPHD3 or control at indicated time points. Four independent experiments (± SEM) are shown (p < 0,05; n = 4). e Analysis of p27 stability in 786–0 cells by cycloheximide chase during reoxygenation after 24 h hypoxia demonstrates markedly increased half-life of p27 upon PHD3 depletion Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Pm, Pm-Or, Rb, RM

Species Glossary

Reactivity: Hu, Mu, Rt, Pm, Pm-Or, Rb, RM

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB100-137AF405
Alexa Fluor 488	NB100-137AF488
Alexa Fluor 532	NB100-137AF532
Alexa Fluor 647	NB100-137AF647
Alexa Fluor 700	NB100-137AF700
Biotin	NB100-137B
CoraFluor 1	NB100-137CL1
DyLight 350	NB100-137UV
DyLight 405	NB100-137V
DyLight 488	NB100-137G
DyLight 550	NB100-137R
DyLight 594	NB100-137DL594
DyLight 650	NB100-137C
DyLight 680	NB100-137FR
DyLight 755	NB100-137IR
FITC	NB100-137F
HRP	NB100-137H
Janelia Fluor 525	NB100-137JF525
Janelia Fluor 549	NB100-137JF549
Janelia Fluor 646	NB100-137JF646
Janelia Fluor 669	NB100-137JF669
PE	NB100-137PE
mFluor Violet 450 SE	NB100-137MFV450
mFluor Violet 500 SE	NB100-137MFV500
mFluor Violet 610 SE	NB100-137MFV610

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NB100-131

HIF-1 alpha Antibody (ESEE122) - BSA Free

(3 Reviews)

(89 Publications)

0.1 ml

NB100-131

Simple Western: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Image shows a specific band for HIF-1 alpha in 0.5 mg/mL of Hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Detection of HIF-1 alpha (red dye 568) in a cultured raw mouse macrophage cell line, using NB100-131. Photos courtesy of Susan Alexander and Hattie Gresham, PhD.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Detection of HIF-1 alpha (red dye) in a cell cytospin from a lavage of a murine skin pouch infected with S. aureus. 100X magnification. Blue: DAPI nuclear staining.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Analysis of a FFPE mouse kidney tissue section using HIF-1 alpha antibody clone ESEE122 at 1ug/mL concentration. The detection was performed using X-cell plus universal HRP polymer detection system with Vector SG chromagen substrate. Image courtesy of a product review by Steven Grover.

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical staining of HIF-1 alpha in normal renal tissue (A) and clear cell renal cell carcinoma (CCRCC) (D). A homogeneous cytoplasmic staining of tubular cells and weak staining in glomerules was observed with HIF-1 alpha (A). In CCRCC, HIF-1 alpha immmunoreactivity was nuclear and/or cytoplasmic (D), while it was perimembranous and/or diffuse cytoplasmic for VEGF-A and VEFG-C (E and F). (magnification x200). Image collected and cropped by CiteAb from the following publication (//www.jeccr.com/content/28/1/40), licensed under a CC-BY license.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Analysis of HIF-1 alpha in paraffin-embedded mouse kidney tissue section using anti-HIF-1 alpha antibody. Image from verified customer review.

<b>Biological Strategies Validation. </b>Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Nuclear HIF-1 alpha protein expression. Xenografts were established in female nude mice (BALB c[nu/nu]) by subcutaneous injection of head and neck squamous cell carcinoma cell lines UT-SCC-2 (UT-2) and UT-SCC-14 (UT-14). Cetuximab (1 mg/injection) or PBS was administered by intraperitoneal injection at day 10, 14, and 17. A tissue microarray was constructed from tumours harvested at day 21, and the expression of nuclear HIF-1 alpha was evaluated by immunohistochemistry (IHC) in untreated controls and cetuximab-treated tumour specimens. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28756482/) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Negative control stain of human placenta (from sea level) using mouse IgG at 1:100. 4uM paraffin-embedded section.

$Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Analysis of a FFPE tissue section of human renal cancer xenograft using HIF-1 alpha antibody (NB100-131 Lot 83115) at 1:200 dilution. The antibody generated a strong cytoplasmic staining mainly in the cancer cells. Only a fraction of cells depicted nuclear staining, while weak to negligible positivity was seen in the tumor stromal cells.$

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - HIF-1 alpha staining in hypoxia-induced human placenta.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Representative immunohistochemical expression for HIF-1alpha, c-Met, CA9 and GLUT1. HIF-1alpha is stained in cytoplasm shown with no staining in normal cervix (A), weak staining intensity in high grade CIN (B), and strong staining intensity in squamous cell carcinoma (C). Scale bar: 50 um. Image collected and cropped by CiteAb from the following publication (//www.translational-medicine.com/content/11/1/185), licensed under a CC-BY license.

Positive immunohistochemical staining for (A) VEGF, (B) HIF-1 alpha , (C) Dll4 (tumor cells), (D) Dll4 (endothelial cells), and (E) CD31 (for microvessel counting, ×200 magnification).

Immunohistochemical analysis in non-GIST STS representing negative, and score 1–3 of CAIX, GLUT-1, HIF-1 alpha , and HIF-2 alpha . non-GIST STS: non-gastrointestinal stromal tumor soft-tissue sarcomas, CAIX: carbonic anhydrase IX, GLUT-1: glucose transporter-1, and HIF-1/2 alpha : hypoxia induced factor 1/2 alpha .

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical analysis in non-GIST STS representing negative, & score 1–3 of CAIX, GLUT-1, HIF-1 alpha , & HIF-2 alpha . non-GIST STS: non-gastrointestinal stromal tumor soft-tissue sarcomas, CAIX: carbonic anhydrase IX, GLUT-1: glucose transporter-1, & HIF-1/2 alpha : hypoxia induced factor 1/2 alpha . Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22454562), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Digital image analysis of cytoplasmic & membranous staining. Cytoplasmic HIF-1 alpha staining is shown (A) & automated image analysis utilizing TissueIA recognizes cytoplasmic HIF-1 alpha staining highlighted in green color (B). CA9 is shown in membranous staining (C) & automated image analysis determines membranous CA9 staining highlighted in green color (D). The output from the algorithm returns a number of quantitative measurements for intensity & percentage of positive staining present. Scale bar: 100 μm. Image collected & cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-185), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical staining of HIF-1 alpha , VEGF-A & VEGF-C in normal renal tissue (A-C) & clear cell renal cell carcinoma (CCRCC) (D-F). A homogeneous cytoplasmic staining of tubular cells & weak staining in glomerules was observed with HIF-1 alpha (A), while VEGF-A & VEGF-C were positive in tubular cells, glomerular mesangium & interstitial macrophages (B & C). In CCRCC, HIF-1 alpha immmunoreactivity was nuclear and/or cytoplasmic (D), while it was perimembranous and/or diffuse cytoplasmic for VEGF-A & VEFG-C (E & F). (magnification ×200). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19302703), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Positive immunohistochemical staining for (A) VEGF, (B) HIF-1 alpha , (C) Dll4 (tumor cells), (D) Dll4 (endothelial cells), & (E) CD31 (for microvessel counting, ×200 magnification). Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/or.2012.2075), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Representative immunohistochemical expression for HIF-1 alpha , c-Met, CA9 & GLUT1. HIF-1 alpha is stained in cytoplasm shown with no staining in normal cervix (A), weak staining intensity in high grade CIN (B), & strong staining intensity in squamous cell carcinoma (C). c-Met (D-F), CA9 (G, H) & GLUT1 (I) shows cell membranous staining. Representative c-Met expression in cervical samples shown with no staining in normal cervix (D), weak membranous staining intensity in squamous cell carcinoma (E) & strong intensity in squamous cell carcinoma (F). CA9 expression showing moderate intensity staining in carcinoma in situ (CIS) (G) & strong staining in adenocarcinoma (H). GLUT1 expression showing strong intensity in squamous cell carcinoma (I). Scale bar: 50 μm. Image collected & cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-185), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Bv, Ca

Species Glossary

Reactivity: Hu, Mu, Rt, Bv, Ca

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-131AF350
Alexa Fluor 405	NB100-131AF405
Alexa Fluor 488	NB100-131AF488
Alexa Fluor 532	NB100-131AF532
Alexa Fluor 594	NB100-131AF594
Alexa Fluor 647	NB100-131AF647
Alexa Fluor 700	NB100-131AF700
Alexa Fluor 750	NB100-131AF750
Biotin	NB100-131B
CoraFluor 1	NB100-131CL1
DyLight 350	NB100-131UV
DyLight 405	NB100-131V
DyLight 488	NB100-131G
DyLight 550	NB100-131R
DyLight 594	NB100-131DL594
DyLight 650	NB100-131C
DyLight 680	NB100-131FR
DyLight 755	NB100-131IR
FITC	NB100-131F
HRP	NB100-131H
Janelia Fluor 525	NB100-131JF525
Janelia Fluor 549	NB100-131JF549
Janelia Fluor 646	NB100-131JF646
Janelia Fluor 669	NB100-131JF669
mFluor Violet 450 SE	NB100-131MFV450
mFluor Violet 500 SE	NB100-131MFV500
mFluor Violet 610 SE	NB100-131MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-131SS
Azide and BSA Free	NBP2-80762

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

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Kit Type

Lysate Subcellular Fraction

Lysate Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

HIF-1 alpha Antibody (H1alpha67)

CHREBP Antibody - BSA Free

iNOS Antibody - BSA Free

CD36 Antibody - BSA Free

GAPDH Antibody - BSA Free

Nox4 Antibody - BSA Free

SR-BI Antibody - BSA Free

IL-1 beta/IL-1F2 Antibody - Azide and BSA Free

RPE65 Antibody (401.8B11.3D9) - BSA Free

Tyrosine Hydroxylase Antibody - Azide Free

EGLN1/PHD2 Antibody - BSA Free

HIF-1 alpha Antibody (ESEE122) - BSA Free