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NB100-105

HIF-1 alpha Antibody (H1alpha67)

(45 Reviews)

(1013 Publications)

0.1 ml

NB100-105

HIF-1 alpha induction by CoCl2 on Caki-1 cell lysate. WB image submitted by a verified customer review.

<b>Biological Strategies Validation and Genetic Strategies Validation.</b>HIF-1 alpha was detected in immersion fixed DFO treated Hela cells (left) but was not detected in HIF-1 knockout HeLa cells (right) using Mouse Anti-human HIF-1 alpha monoclonal antibody (Catalog # NB100-105) at 25 ug/mL for 3 hours at room temperature. Cells were stained using a NorthernLights (TM) 557-conjugated Donkey Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to nuclei.

<b>Biological Strategies Validation and Genetic Strategies Validation.</b>Naive CD4 T cells from WT, VHL-deficient (Vhl KO), or HIF-1 alpha-deficient (HIF-1 alpha KO) mice were differentiated under IL-22-skewing conditions for a total of 60 h. Some cells remained at normoxia for the duration of the culture (N); others were at normoxia for 35 h and then hypoxia (1% O2) for 24 h (H). At 60 h, nuclear extracts were harvested, and HIF-1 alpha and Lamin B1 levels were analyzed by Western blot. Image from verified customer review.

Analysis using the Alexa Fluor (R) 488 conjugate of NB100-105. Staining of HIF-1 alpha in multiple myeloma cells: H929 cells (0.5 x 10^6) were stained with Alexa Fluor 488(R) conjugated HIF-1 alpha antibody (NB100-105AF488). Image courtesy of Dr. Barbara Muz at Washington University in St. Louis School of Medicine.

Staining of HIF-1 alpha in human kidney using NB100-105. Renal tubular epithelium showed moderate membranous, cytoplasmic and nuclear staining, and glomeruli showed faint to moderate nuclear staining.

HIF1alpha/PFKFB3 is upregulated in beta-cells of HIP rats and humans with type 2 diabetes. Representative Western blot of PFKFB3 and HIF1alpha levels in nuclear-enriched- and whole cell extracts from non-diabetic (ND) and T2D donor islets. Data are presented as mean +/- SEM, n = 3 independent biological samples for each group. Statistical significance was analyzed by Student t-test (*p 80% of endogenous Sin1 while levels of myc-FL Sin1 associated with Rictor are comparable with endogenous Sin1 levels. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GRPs enhance axonal growth in DRGs in vitro. A–C, Representative montage images are shown for control dissociated DRG culture (A), dissociated DRGs cocultured with rat GRPs (B), and dissociated DRGs cultures exposed to conditioned medium from alkaline phosphatase-expressing rat GRPs (C). beta III-tubulin (red) immunofluorescence highlights the neurons; GRPs are visualized by immunostaining for alkaline phosphatase (green). D shows quantification for the average length of the longest axon per neuron ± SEM (n ≥ 30 neurons in three separate experiments; **p ≤ 0.01 by Student’s t test). Scale bar, 250 μm. Image collected and cropped by CiteAb from the following open publication (//www.eneuro.org/lookup/doi/10.1523/ENEURO.0171-16.2017), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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

Inhibition of CIP2A by siRNA impeded cell viability and DNA synthesis in HPV‐16E6–expressing cells. A, Elevated expression of CIP2A protein in 16E6‐expressing RPE1 cells. B, Western blot analysis of CIP2A and p53 proteins after transfection with scrambled siRNA (siCon) or CIP2A siRNA (siCIP2A) for 48 h. A representative of 3 independent experiments is shown. C, Cell viability assay of RPE1‐16E6 cells with CIP2A knockdown. D, Representative flow cytometry of BrdU staining profiles is shown. E, The mean and SD of BrdU‐positive cells from 3 experiments are summarized. **, P 30°. Scale bars represent 5 μm.(B) Representative graph of delta KT, delta MT, and the difference between delta KT and delta MT through time in a lateral kinetochore assessed from movie stills as in (A).(C) Graph of attachment state transitions experienced by percentage of lateral kinetochores, within a 50 s window, measured from time-lapse movies of cells transfected with siRNA oligos as indicated and treated with monastrol for 1 hr prior to imaging.(D) Graph of interkinetochore distances describing fate of three randomly chosen kinetochores from conditions described in (A).(E) Cumulative graph and T50 table showing lifetime of lateral kinetochores in HeLa cells treated with either control or MCAK siRNA or HeLa cells expressing tetracycline-inducible siRNA-resistant HEC1Ndc80-delta loop-YFP as indicated. The dashed line marks T50, the period when 50% of lateral kinetochores had ceased to remain laterally attached.(F) Representative immunofluorescence images of control or MCAK siRNA-transfected cells treated with monastrol for 1 hr prior to fixation and immunostained with antibodies against astrin and tubulin and CREST antisera and stained with DAPI for DNA. Insets are 3× magnified. Scale bars represent 5 μm (insets, 2 μm).(G) Graph of the percentage of lateral kinetochore pairs with both, one, or none of the pair displaying astrin in cells treated as in (F).(H) 3D-rendered images are rotated (as indicated) showing a lateral kinetochore in MCAK siRNA-treated cells immunostained with antibodies against astrin (red) and beta -tubulin (green) and CREST antisera (blue). The blue arrow marks kinetochore attachment site and pink arrow marks the plus end of laterally interacting microtubules. Scale bars represent 2 μm.p values representing significance levels were obtained with the Mann-Whitney U test (C), proportion test (D and F), and paired sample t test (E). ∗ and # indicate significant and insignificant differences, respectively. See also Figure S4. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23891108), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

UBC9 is degraded by autophagy in epithelial cells.(A) Immunolocalization of UBC9 in ultrathin sections of HKs transduced with empty or HPV16 E6/E7 vectors. Original view (left) and higher magnification (right) of boxed regions. Gold particles are selectively enriched in autophagic structures highlighted by arrows. Scale bar = 1 μm. (B) Top: Representative WB of HaCaT cells treated with the indicated autophagic activators (left) and inhibitors (right). Activation of autophagy was monitored by the conversion of LC3 (LC3-I) to the lipidated LC3 (LC3-II) form, a marker of autophagosome production induced by autophagic stimuli [41]. LC3-II accumulation was used to verify autophagic impairment [41]. Bottom: normalized UBC9 expression. Data are expressed as fold over untreated cells. Bars represent means ± SEM of n = 4 different biological replicates. ns: not significant (Kruskal–Wallis one-way ANOVA with Dunn’s post hoc test) compared to vehicle control groups. (C) Representative WB analysis of U-2 OS or MCF7 cells treated with chloroquine. n = 3 different biological replicates. (D) Representative WB analysis of MCF7 cells transduced with scramble or ATG5 shRNA. The observed ATG5 band represents the ATG5-ATG12 conjugated form. LC3-I accumulation is reported to evidence autophagic deficiencies promoted by shATG5. n = 3 replicates of a single transduction. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.ppat.1006262), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Fe, Ma, Pm, Pm, Rb, Sh, Xp

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Fe, Ma, Pm, Pm, Rb, Sh, 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	NB100-105AF350
Alexa Fluor 405	NB100-105AF405
Alexa Fluor 488	NB100-105AF488
Alexa Fluor 532	NB100-105AF532
Alexa Fluor 594	NB100-105AF594
Alexa Fluor 647	NB100-105AF647
Alexa Fluor 700	NB100-105AF700
Alexa Fluor 750	NB100-105AF750
Allophycocyanin	NB100-105APC
Biotin	NB100-105B
DyLight 350	NB100-105UV
DyLight 405	NB100-105V
DyLight 488	NB100-105G
DyLight 550	NB100-105R
DyLight 594	NB100-105DL594
DyLight 650	NB100-105C
DyLight 680	NB100-105FR
DyLight 755	NB100-105IR
FITC	NB100-105F
HRP	NB100-105H
Janelia Fluor 549	NB100-105JF549
Janelia Fluor 646	NB100-105JF646
PE	NB100-105PE
PerCP	NB100-105PCP
mFluor Violet 450 SE	NB100-105MFV450
mFluor Violet 500 SE	NB100-105MFV500
mFluor Violet 610 SE	NB100-105MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Azide and BSA Free	NBP2-80760

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NB100-479

HIF-1 alpha Antibody - BSA Free

(28 Reviews)

(497 Publications)

0.1 ml

NB100-479

ChIP-qPCR assay of HIF-1 binding to hypoxia response element (HRE) of the PKM2 gene in human MDA-MB-231 breast cancer cells treated with vehicle or DMOG (HIF inducer) for 8 hours. Negative control: immunoprecipitation was performed with IgG. Image courtesy of Gregg Semenza, Johns Hopkins University School of Medicine.

<b>Biological Strategies Validation. </b>Normoxic pre-treatment sensitizes glioma cells to radiation after graded chronic hypoxic (GCH) exposure. The results of anchorage-independent colony forming assays are shown for U87, U87-luc, GL261 glioma cells and 0308 GSCs after 5 Gy radiation exposure under varying O2 conditions. For easier comparisons among cell types, raw values are expressed as a % of the cell type's negative (non-irradiated) control and the means & SEMs are plotted. Each result represents at least 3 independent samples, plated in triplicate. Holm-Sidak comparisons for multiple groups were used for statistical comparisons of raw values (*p0.05. (d) IDH1R132H expression diminishes DEPTOR levels. Flag-IDH1R132H was introduced in p53−/− MEFs by retroviral transduction and whole-cell lysates immunoblotted. (e) Inhibition of endogenous mutated IDH1R132C decreases mTOR activity in a KDM4A-dependent manner. HT1080 cells were transduced with lentivirus expressing sh_KDM4A.3 or sh_Control. The cells were treated with 3 μM AGI-5198 twice every day for 5 days and whole-cell lysates blotted for markers of mTOR activation. (f) Expression of mutant IDH1 in NHA-hTERT increases mTOR signalling. IDH1WT-Flag or IDH1R132H genes were introduced in astrocytes through retroviral infection and cell lysates were blotted for mTORC2 activation. (g) IDH1R132H overexpression increases 2HG production in astrocytes. Intracellular 2HG levels were normalized to glutamate. Asterisk denotes a statistical difference between IDH1R132H and empty vector cells, two-sided t-test P<0.0001 (graph represents three independent experiments). Error bars represent standard deviation. (h) Treatment of NHA-hTERT with octyl-2HG activates mTOR signalling. The cells were treated for 8 h with 1 mM octyl-2HG. The experiment shown is a representative of triplicates. (i) Non-canonical mTOR activation in IDH1/2WT and IDH1R132H human astrocytomas. Scale bar, 50 μm. Representative samples from IDH1/2WT (n=3) and IDH1R132H (n=3) human astrocytomas are shown. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/ncomms12700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Comparison between primary tumor and mLNs of the mouse model. Expression of CA9 and GGT1 in mLNs was higher than that in the primary tumor at 1week after injection of cells. (A) CA9 and GGT1 expression of HT29 mLNs compared to primary tumor at 6 weeks or 1 week after injection of cells. (B) Tissue oxygen concentration (%) of rectal submucosa (SM) and nLNs (n = 3). Error bars represent SD. mNs: metastatic lymph nodes, nLNs: non metastatic lymph nodes. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30542087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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

Hif1 alpha expression in neonatal and adult testis.(A) Section of testis from 5-day old (P5) male new born pups showing Hif1 alpha expression in MVH+ gonocytes within the seminiferous tubules (top) and negative control images without primary antibodies (bottom). Scale bar: 50μm. (B) Western blot analysis of Hif1 alpha expression in P5 testes (left) compared to extract of the adult brain sub-ventricular zone (SVZ) (right). Loading control ( beta -Actin) is shown below. (C) Section of adult (3 month old) testis showing Hif1 alpha expression in spermatogonia. Scale bar: 30μm. (D) Western blot analysis of whole adult testis. HEK293 cells treated with DFX were used as a positive control and intestinal tissue was used as a negative control. Loading control ( beta -Actin) is shown below. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27148974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Subcellular localization of mPARM-1 and hPARM-1 (full-length and mutant proteins). (a) NIH/3T3 cells, transiently transfected with GFP-tagged mParm-1 or hParm-1 constructs were visualized using confocal microscopy. (b) For the Golgi co-localization, transfected NIH/3T3 cells were fixed and stained with Bodipy ceramide marker. For late and early endosomes co-localization, fixed cells were labeled with (c) anti-Rab5 (early endosomes (1:100, Cell signaling)) and (d) anti-Rab7 (late endosomes (1:100, Cell signaling)) antibodies, respectively. Jurkat T cells, transiently transfected with hParm-1-GFP proteins were visualized (e) without fixation or (f) following fixation and staining with CellMask plasma membrane labeling. NIH/3T3 cells were transiently transfected with (g) ∆EC-GFP, (h) ∆SP-GFP, (i) EC-GFP, (j) ∆TM-GFP and (k) ∆CT-GFP constructs of hPARM-1 and visualized using confocal microscopy. (l) hPARM-1-GFP co-localizes with microtubules. NIH/3T3 cells transfected with hParm-1-GFP construct were fixed and stained with anti-alpha -tubulin (1/2000, Sigma) antibody. Arrows indicate co-localized hPARM-1-GFP vesicles and microtubules. NIH/3T3 cells transiently expressing (m) hPARM-1-GFP or (n) ∆CT-GFP were fixed, immunostained for caveolin-1 (1:100, Novus Biologicals), and examined by confocal fluorescence microscopy. For hPARM-1-GFP-caveolin-1 co-localization, cells that clearly demonstrated cell membrane PARM-1 localization were chosen. All co-localizations were observed following merging images of GFP-tagged proteins with those of Golgi, endosomes, plasma membrane, alpha -tubulin or caveolin-1 labeling. Cells were imaged with a laser-scanning confocal microscope (Bio-Rad MRC-1024 ES) mounted on a Nikon TE-300 using a Plan Apochromat 60x (NA 1.40) oil objective (Nikon), digitally acquired using Laser Sharp software Version 3.2 (Bio-Rad). For live cell imaging, signals were collected at a rate of 2 seconds. Images were analyzed using NIH ImageJ Version 1.42l software. Data are representative of 3 independent experiments. Image collected and cropped by CiteAb from the following open publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-12-84), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Inhibition of Cdk1 and Cdk2 by CIP2A knockdown in cervical cancer SiHa cells caused G1 arrest. A, Western blot analysis of 16E6, p53 and CIP2A after HPV‐16E6 knockdown in cervical cancer SiHa cells. B, Protein expression of CIP2A, B‐Myb, Cdk1 and Cdk2 in SiHa cells after CIP2A knockdown. Data from a representative of 3 experiments are shown. C, Flow cytometric analysis of SiHa cells with CIP2A knockdown treated with PBS or bleomycin. A representative flow cytometry of 3 independent experiments is shown. D, Quantification of percentages G1 phase cells. Data from 3 experiments are summarized. *, P < .05 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29893470), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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

Reactivity:

Hu, Mu, Rt, Po, Ca, Fi, Gt, Ha, Pm, Rb, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Fi, Gt, Ha, Pm, Rb, Ze

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-479AF350
Alexa Fluor 405	NB100-479AF405
Alexa Fluor 488	NB100-479AF488
Alexa Fluor 532	NB100-479AF532
Alexa Fluor 594	NB100-479AF594
Alexa Fluor 647	NB100-479AF647
Alexa Fluor 700	NB100-479AF700
Alexa Fluor 750	NB100-479AF750
Allophycocyanin	NB100-479APC
Allophycocyanin/Cy7	NB100-479APCCY7
Biotin	NB100-479B
DyLight 350	NB100-479UV
DyLight 405	NB100-479V
DyLight 488	NB100-479G
DyLight 550	NB100-479R
DyLight 594	NB100-479DL594
DyLight 650	NB100-479C
DyLight 680	NB100-479FR
DyLight 755	NB100-479IR
FITC	NB100-479F
HRP	NB100-479H
Janelia Fluor 549	NB100-479JF549
Janelia Fluor 646	NB100-479JF646
PE	NB100-479PE
PE/Atto594	NB100-479PEATT594
PE/Cy5.5	NB100-479PECY55
PE/Cy7	NB100-479PECY7
PerCP	NB100-479PCP
mFluor Violet 450 SE	NB100-479MFV450
mFluor Violet 500 SE	NB100-479MFV500
mFluor Violet 610 SE	NB100-479MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-479SS

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NB100-1028

AIF-1/Iba1 Antibody

(21 Reviews)

(395 Publications)

0.1 mg

NB100-1028

GM1 effects on brain microglia in vivo, after peripheral administration of LPS. Immunoblot in whole brain lysates and densitometric analysis show LPS-dependent increase in AIF-1/Iba1 expression. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34991625/) licensed under a CC-BY license.

Reactive microglia (green) in peritumoral area of IC injected human glioblastoma cells in mouse brain. NeuN (red), DAPI (blue). Antibody at 1:250. IHC image submitted by a verified customer review.

AIF-1/Iba1 in canine brain. Primary antibody used at 1 ug/mL and incubated with tissue for 30 minutes at room temperature. IHC-P image submitted by a verified customer review.

Staining in mouse brain using AIF-1/Iba1 Antibody. IHC-P image submitted by a verified customer review.

Brown arrow= AIF-1/Iba1 positive cells, Green arrow= mTOR positive cells, Black arrow= mTOR and AIF-1/Iba1 positive cells. IHC-P image submitted by a verified customer review.

Staining in rat hippocampus using AIF-1/Iba1 Antibody. IHC-Fr image submitted by a verified customer review.

Feline optic nerve microglia were immunolabeled with AIF-1/Iba1 Antibody (green), DAPI (blue). Imaging was performed using an epifluorescence microscope. IHC-Fr image submitted by a verified customer review.

Mouse dorsal root ganglia. AIF-1/Iba1 expression in reactive macrophages. Maximum intensity z-projection from 3D images. IHC image submitted by a verified customer review.

Staining in mouse brain using AIF-1/Iba1 Antibody. IHC image submitted by a verified customer review.

Analysis of LPS injected mouse brain tissue, 20 um thickness, frozen. Primary antibody dilution, 1:200. Secondary antibody CY3. Mounted with DAPI mount. Image from verified customer review.

AIF-1/Iba1 staining of AD mouse model (hippocampus). Image from verified customer review.

Negative Control showing staining of paraffin embedded Human Spleen, with no primary antibody.

(0.1ug/ml) staining of Mouse Lymph node lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.

(1ug/ml) staining of Human Frontal Cortex (A) and (0.1ug/ml) Mouse (B) and Rat (C) Brain lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.

(8ug/ml) staining of paraffin embedded Human Spleen. Heat induced antigen retrieval with citrate buffer Ph 6, HRP-staining.

GM1 effects on brain microglia in vivo, after peripheral administration of LPS. C) Immunoblot in whole brain lysates and densitometric analysis show LPS-dependent increase in Iba 1 expression. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34991625), licensed under a CC-BY licence.

CXCR2+neutrophils are not required for microglial activation. a Representative images of Iba1 immunohistochemistry staining in lumbar spinal cord ventral horns of naive control, control EAE, and Cxcr2 cKO EAE mice. Quantitative analysis of Iba1+ cell (b) soma area as shown in a. A total of 2338 Iba1+ cells were included in our analyses of soma size (cont naive, 222 Iba1 cells; control EAE, 1236 Iba1+ cells; Cxcr2 cKO EAE, 880 Iba1+ cells). Control naive, n = 3; control EAE, n = 3; Cxcr2 cKO EAE, n = 3. *p 1.5, FDR-corrected p1.5, FDR-corrected p<0.05) to identify GO terms, including inflammatory response (b). The volcano plot shows significant DEGs derived from the NanoString analysis of the brains of Plcg2 inactivation (PLCG2 inact, n=3) and WT (n=3) mice (1-month male) (c). Immunostaining of microglial markers with IBA1 (green) and P2RY12 (red) and quantification of percent area in brain sections of 1-month-old male WT and PLCG2 inact demonstrate unchanged microglial morphology and area coverage (d). GO gene ontology, BP biological process, DEGs differentially expressed genes, FDR false discovery rate Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35180881), licensed under a CC-BY licence.

Deficiency of HDAC3 in microglia suppresses the cGAS-STING-mediated autoimmune response. (K) Proteins extracted from the ischemic penumbra and contralateral cortex of HDAC3 cKO and WT mice subjected to tMCAO 6 h post-reperfusion were analyzed with antibodies against cGAS, HDAC3, Iba1, and GAPDH. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32863951), licensed under a CC-BY licence.

ADT induced SPINK1 upregulation associates with NE-phenotype in mice and NEPC patients.a Box plots depicting relative expression of SPINK1, SYP, CHGA, TUBB3, and VIM transcripts (read counts) in VCaP tumors implanted orthotopically in orchiectomized mice and subjected to vehicle (n = 4) or anti-androgens [enzalutamide (n = 4) or ARN-509 (n = 4)] treatment for 4 weeks (GSE95413). b Representative images of immunohistochemical staining for the same markers shown in a using VCaP xenograft tumors as described in a. Scale bar represents 100 μm. c Box plots depicting quantification of the immunohistochemical staining in VCaP xenografts for the markers shown in b. d Representative images for immunohistochemical staining of SPINK1, SYP, CHGA, and TUBB3 in 22RV1 xenograft tumors excised from orchiectomized mice treated with enzalutamide (20 mg/kg body weight) or vehicle control (n = 5 each). Intact group represents non-castrated control mice (n = 5). Scale bar represents 50 μm. e Box plots depicting quantification of the immunohistochemical staining in 22RV1 xenografts for the markers shown in d. f Representative images showing H&E staining (×200 magnification) and immunostaining (×200 magnification) for AR, synaptophysin, and SPINK1 in tumor specimens obtained from NEPC patients’, namely WCM12, WCM155 (an organoid), and WCM677. Scale bar represents 100 µm. Data are presented as box-and-whisker plots with median, where the box extends from 25th–75th percentile, and whiskers ranges from minimum and maximum values. For panels a, c, e one-way ANOVA, Dunnett’s multiple-comparisons test was applied. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31959826), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines and EBV positive BLs. a Representative western blots illustrating the expression of MTH1, OGG1, and MUTYH in pairs of EBV-negative and -positive cell lines. GAPDH was used as loading control. b Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Mean ± SE of four independent experiments. c Representative western blots illustrating the expression of EBNA1, MTH1, OGG1, and MUTYH in the Mutu cell lines. d Densitometry quantification of expression in the EBV positive cell lines relative to the EBV-negative Mutu-30. Mean ± SE of four independent experiments Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Rab31 expression levels in stably transfected breast cancer cells. (A) pAb RT3-IgG specifically detects rab31 in cell lysates from stably transfected MDA-MB-231 and CAMA-1 breast cancer cells in Western blot analyses. Vector control, MDA-MB-231, or CAMA-1 cells were stably transfected with the empty vector pRcRSV; batch, parental MDA-MB-231 (low endogenous rab31 expression) or CAMA-1 (no endogenous rab31 expression) cells were stably transfected with the pRcRSV-based rab31 expression vector; high, medium or low, selected cell clones of batch-transfected MDA-MB-231 or CAMA-1 cells with differing high, medium or low protein levels of rab31. (B) Rab31 antigen values (ng/mg of total protein) in rab31-transfected MDA-MB-231 and CAMA-1 cells, determined by rab31-ELISA. Mean values (± SEM) of at least three independent experiments are depicted. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/22920728), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

EGFR inhibition downregulates VEGF and HIF-1 in vitro and in vivo.SQ20B cells were seeded at 25% confluence and cultured overnight. The next morning, cells were transfected with 150 nanomoles siRNA (either EGFR SmartPool or control non-targeted) in Optimem transfection medium using Oligofectamine. After 24 hours, the transfection medium was replaced with fresh, prewarmed culture medium. 24 hours after this (48 hours after transfection), cells were exposed to either 21% or 1% oxygen. Three hours later they were harvested and Western blotting was performed. (B) SQ20B cells were treated with 10 nM cetuximab or DMSO (control) for 16 hrs, and then exposed to either 21% or 1% oxygen. Three hours later they were harvested and Western blotting was performed. (C) Nude mice were injected subcutaneously in the flank with SQ20B cells to form xenografts. When the tumors reached a size of 100–150 mm3 (approximately 7–10 days after injection), half the mice (lanes 4–6) were started on an erlotinib-containing diet (50 mg/kg/day). After 4 days of feeding, mice were sacrificed, and the tumors were removed. Half of each tumor was lysed in protein lysis buffer, and Western blotting was performed for pAkt (S473) and HIF-1 alpha . Each lane represents a tumor from a different mouse. (D) The other half of each tumor from (E) was homogenized in PBS, and then ELISA for VEGF was performed. VEGF level was normalized to tumor weights. Data shown represent mean values from 3 control mice and 3 erlotinib-treated mice. Error bars represent standard error of the mean. p value was obtained using Student's t-test. (E) H226 cells were treated with 10 µM erlotinib or DMSO (control) for 16 hrs, and then exposed to either 21% or 1% oxygen. Three hours later they were harvested and Western blotting was performed. (F) H226 cells were seeded then later that day they were treated with erlotinib (10 µM) or DMSO (control). 24 hours later, the media was changed and replaced with media containing 1% serum with or without erlotinib. Cells were exposed to 1% oxygen. 16 hours later, aliquots of supernatant were removed from dishes, and ELISA for VEGF was performed. ELISA values were normalized to the number of cells present. Data shown represent mean values. Error bars represent standard error of the mean. p value was obtained using Student's t-test. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/19657384), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Elevated levels of additional proteins and GM3 ganglioside in the MEC of MPS IIIB brain.Staining performed with antibodies to the indicated substances was observed in the MEC region of 3 month-old MPS IIIB mice (for total ubiquitin and polyubiquitin) and 6 months for all others. Staining was not seen in the MEC region of age-matched control mice (Naglu +/−) nor in the LEC region of MPS IIIB mice (the latter not shown). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0027461), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ERK2 utilizes kinase-docking domains to interact with ATG5–ATG12 and LC3-II.(a) Mutations in FRS on ERK2 decrease colocalization of ERK2 with ATG5–ATG12, LC3 and WIPI1. Immunofluorescence (IF) showing colocalization (depicted as white pixels by ‘colocalization finder application’) of WT-ERK2-HA, FRS ERK2 mutants (L198A-, L232A-, L198A/L232A-, Y261A-ERK2-HA) or common docking (CD) mutant (D319N-ERK2-HA) with ATG5–ATG12 (panels 1–6), LC3 (panels 7–12) or WIPI1 (panels 13–18) in EGF-treated NIH/3T3 cells. ERK2 is stained in red, and autophagy proteins are stained in green. Scale bar, 10 μm. The bars represent mean±s.e.m. **P<0.01, ****P<0.0001 compared with WT-ERK2-transfected cells; Student’s t-test, 50 cells analysed from n=2. (b) Mutations in FRS on ERK2 decrease colocalization of ERK2 with nuclear ATG5–ATG12 or LC3. IF showing colocalization (white pixels) of WT-ERK2-HA (red), FRS ERK2 mutants (L198A-, L232A-, L198A/L232A-, Y261A-ERK2-HA) or common docking (CD) mutant (D319N-ERK2-HA) with ATG5–ATG12 (panels 1–6) or LC3-II (panels 7–12) in EGF-treated NIH/3T3 cells. Scale bar, 5 μm. The bars represent mean±s.e.m. **P<0.01, ***P<0.001, ****P<0.0001 compared with WT-ERK2-transfected cells; Student’s t-test, 50 cells analysed from n=2. Arrows depict colocalization. (c) ATG5–ATG12 conjugation is required for ERK phosphorylation. Immunoblots for P-ERK, total ERK and beta -actin in NIH/3T3 cells transfected with WT ATG5 or the conjugation-defective ATG5 K130R mutant and treated with EGF (10 min). The bars represent mean±s.e.m. *P<0.05 compared with WT ATG5-transfected cells; Student’s t-test, n=3. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/ncomms3799), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Human tumor microarrays (TMAs).Pilocytic astrocytoma TSPO immunohistochemistry (A) and TSPO immunohistochemical scoring (C). Glioblastoma multiforme TSPO immunohistochemistry (B) and TSPO immunohistochemical scoring (D). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0141659), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

DNMT1 reveals a SCMC-like cortical localization with aberrant localization in Nlrp2tm1a/tm1a derived oocytes.(A) Whole mount immunofluorescence co-staining with anti-DNMT1 and DAPI on the same Nlrp2M+/Z+ embryos used to stain NLRP2 reveals a SCMC-like cortical localization of DNMT1 with a diffuse nuclear stain in later stage embryos. Scale bar represented is 200 μm. (B) DNMT1 staining in paraffin embedded oocyte sections reveals a less cortical, more cytoplasmic intense stain with nucleolar focus in oocytes from Nlrp2tm1a/tm1a dams compared to oocytes from Nlrp2+/+ dams. (C) Whole mount immunofluorescence for DNMT3A in unfertilized control oocytes reveals a characteristic metaphase associated localization and no difference is noted in oocytes derived from Nlrp2tm1a/tm1adams. (D) Whole mount immunofluorescence in unfertilized oocytes reveals that as expected, DNMT3B is not yet expressed in unfertilized control oocytes and no expression is noted in oocytes derived from Nlrp2tm1a/tm1adams. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep44667), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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

TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 and MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 and MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) and both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 and MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); and mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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NB100-449

HIF-1 alpha Antibody

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NB100-449

Simple Western: HIF-1 alpha Antibody [NB100-449] - Simple Western lane view 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.

Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Mouse Brain, Neurons 40X

Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1-alpha by immunohistochemistry. Sample: FFPE section of renal cell carcinoma. Antibody: Affinity purified rabbit anti-HIF1-alpha antibody (NB110-58773). Detection: DAB

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of Human HIF-1 alpha by Western Blot and Immunoprecipitation. Samples: Whole cell lysate (5, 15 and 50 ug for WB; 1 mg for IP, 20% of IP loaded) from HeLa cells that were either treated with cobalt chloride (+; 200 uM) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody used for WB at 0.1 ug/mL(A) and 1 ug/mL (B) and used for IP at 3 ug/mg lysate. HIF-1 alpha was also immunoprecipitated by a previous lot of this antibody. Detection: Chemiluminescence with exposure times of 30 seconds (A) and 10 seconds (B).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Blot showing the effect of hypoxia on the protein expression levels of the purine biosynthetic enzymes. HIF-1 alpha is stabilized in hypoxia as expected, and no significant increase in the purine enzymes was detected between normoxic (21% oxygen) and hypoxic (1% oxygen) growth conditions. The positions of molecular markers surrounding each band of interest are shown for each blot. ADSL (NBP2-03107), ATIC (NBP2-01941), FGAMS (NBP1-84691), GART (H00002618-M01), HIF-1a (NB100-449), PAICS (NBP2-02817), PPAT (NBP2-02056). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32439803/) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Murine primary bone marrow derived macrophages stained with HIF1-alpha antibody (red). Nuclei were counterstained with DAPI (blue). Image from verified customer review.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody [NB100-449] - Analysis of microvascular density and HIF-1alpha activity. Low, homogenous expression of HIF-1alpha was detected in the tumors of NNK treated mice (40X, scale bar = 25 um). Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license.

Flow Cytometry: HIF-1 alpha Antibody [NB100-449] - HeLa cells were treated for 15 hrs with 200 uM CoCl2, fixed in PFA, and permeabilized in 90% MeOH. 1 X 10^6 cells were stained with 0.125 ug anti-HIF-1 alpha and secondary FITC-conjugated goat anti-rabbit (in a 150 uL reaction). Black: treated, anti-KLH control IgG; Red: untreated, anti-HIF-1 alpha; Blue: treated, anti-HIF-1 alpha.

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of HIF-1 alpha in human myeloma cell lysate using anti-HIF-1 alpha. Cells were untreated or treated with IGF-1, IL-6 or CoCl2. Image from verified customer review.

Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of HIF-1 alpha in a hypoxic sample. Lane 1: CoCl2 treated Cos-7 nuclear extract (hypoxic). Lane 2: Untreated Cos-7 nuclear extract (normoxic).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of mouse HIF-1 alpha on hypoxia treated MEFs

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Samples: Whole cell lysate (5, 15 and 50 ug) from HeLa cells that were treated with cobalt chloride (+; 200 uM) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with exposure times of 30 seconds.

Western Blot: HIF-1 alpha Antibody [NB100-449] - BMDM were seeded at 0.5x10^6 overnight. Cells were treated with 10 ng/ml LPS for 24 hrs. Image from verified customer review.

Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of total protein using anti-HIF-1 alpha, -CAIX, -ISCU antibodies and VDACs antibody (PMID: 29596470).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of total protein using anti-HIF-1 alpha, -ISCU, -FXN antibodies. CoCl2 was used to treat or not HeLa cells for 2 days (PMID: 29596470).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1 alpha by western blot. Samples: Whole cell lysate (15 and 50 ug) from HEK293T cells that were either treated with 200 uM cobalt chloride (+) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with exposure times of 3 minutes.

Western Blot: HIF-1 alpha Antibody [NB100-449] - 3T3-L1 mouse embryonic fibroblast adipose-like cell line. Antibody at 1:2000. WB image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Formaldehyde-fixed asynchronous HeLa cells.

Immunoprecipitation: HIF-1 alpha Antibody [NB100-449] - HIF-1 alpha analysis in HEK293 cells. Image from verified customer review.

Immunoprecipitation: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1 alpha by western blot of immunoprecipitates. Samples: Whole cell lysate (1 mg for IP, 20% of IP loaded) from HEK293T cells that were treated with 200 uM cobalt chloride. Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 1 ug/ml and for IP at 6 ug/mg lysate. Detection: Chemiluminescence with exposure times of 3 minutes.

beta -Glucan size affects the requirement for reactive oxygen species (ROS) in IL-1 beta induction.(B) Human mDCs from healthy donors or chronic granulomatous disease (CGD) patients were stimulated with curdlan or glucan-mp for 8 h. HIF-1 alpha and pro-IL-1 beta protein expression measured by immunoblot (n = 2 donors).

Hypoxia downregulates CFTR expression. (e) Western blot showing the expression changes of HIF-1alpha and EMT markers induced by hypoxia in MDCK cells, quantification analysis is shown in the lower panel, *p < 0.05; (Full-length blot is shown in Supplementary Figure S7d.). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28701694), licensed under a CC-BY licence.

BCAT1 expression and inhibition in human macrophages. (e) Western blot analysis of IRG1, IL-1beta, HIF-1alpha and beta-actin (ACTB) in control (untreated), ERG240-treated (20 mM, 3 h), LPS treated (100 ng ml-1, 3 h) and LPS+ERG240 treated (LPS, 100 ng ml-1; ERG240, 20 mM for 3 h) hMDMs. The experiment is representative of three independent experiments using n=3 healthy donor hMDMs each. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms16040), licensed under a CC-BY licence.

Elevated PIK3/AKT/HIF-1alpha pathways in KL SqCC tumours. (c) IHC analysis (top) and quantification (bottom) of p63, p-AKT, p-S6, p-4EBP1, HIF-1alpha and GLUT1 in KL tumours (n=6 each group). Two-tailed t-test, ****P<0.0001, ***P<0.001, **P<0.01. Scale bar, 50 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28548087), licensed under a CC-BY licence.

Adenosine mediates increase in pro-IL-1beta via a HIF-1alpha-dependent pathway. (h) LPS primed PECs obtained from HIF-1alpha-cKO and control mice were treated with or without NECA at different time points as indicated followed by pulsing with ATP. Cell lysates were collected after ATP pulsing. HIF-1alpha, pro-caspase-1, Caspaspe-1 and pro-IL-1beta was measured in cell supernatant by western blot. Immunoblots shown are representative results from at least three independent experiments. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24352507), licensed under a CC-BY licence.

Morphological alterations induced by DMOG are HIF-1alpha dependent. (A) glEND.2 cells were stably transfected with shGFP, shHIF-1alpha or shHIF-2alpha. The clones were cultured under normoxic (N) or hypoxic (H, 1% O2) conditions, or treated with DMOG (D, 1 mM) for 6 h. 30 ug protein of cellular protein were loaded for the detection of HIF-1alpha, and nuclear extracts (20 ug protein) were used for the detection of HIF-2alpha. Image collected and cropped by CiteAb from the following publication (//biosignaling.biomedcentral.com/articles/10.1186/1478-811X-11-80), licensed under a CC-BY licence.

Pyruvate kinase isoform M2 (PKM2) and hypoxia-inducible factor 1alpha (Hif-1alpha) bind directly to the promoter region of PDL1 in primary murine BMDM cells. BMDM cells were treated with TEPP-46 at 50 uM for 1 h prior to stimulation with LPS (100 ng/ml, 24 h) (C) Sequential ChIP assays measuring simultaneous endogenous binding of PKM2 and Hif-1alpha to chromatin in response to LPS (100 ng/ml, 24 h) +/-TEPP-46 (pretreatment using 50 uM, 60 min). ChIP data are calculated as percent of input, error bar represents mean +/- SEM, and statistics are performed as two-tailed unpaired t-test *P < 0.05, **P < 0.01, and ***P < 0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29081778), licensed under a CC-BY licence.

Changes in Hepatic Oxygen Saturation and Hypoxia-related Protein Expression. (C) In the Western blot analysis, the experimental group was relatively higher expression of hypoxia-inducible factor-1alpha (HIF-1alpha) and vascular endothelial growth factor (VEGF) protein than the control group at eight weeks. The full-length blots with these antibodies were presented in supplementary Figure S1. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29079853), licensed under a CC-BY licence.

Effects of cell stress on VEGF-A and HIF1alpha expression in Muller cells and Y79 photoreceptors. (B) Western blots for HIF1alpha using cellular proteins, n = 4/group, ** p < 0.01. For MIO-M1 Muller cells: Grey bars: 5 mM glucose. Black bars: 25 mM glucose. For Y79 photoreceptors: Grey bars: 11 mM glucose. Black bars: 25 mM glucose. NS, not significant; LG, low glucose; HG, high glucose. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/18/3/533), licensed under a CC-BY licence.

Hypoxic conditions upregulate CNN3 in BeWo cells.BeWo cells were cultured either under normoxic or under hypoxic conditions for 24hr. (A) Total protein lysates were examined with the Western Blot technique to detect CNN3 protein levels. For normalization, HPRT was stained on the same membrane. As hypoxia marker, HIF-1 alpha was detected as well. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25050546), licensed under a CC-BY licence.

Phenylhydrazine administration results in hypoxia in retinal vessels and in HIF-1alpha and HIF-2alpha stabilization in peripheral blood leukocytes. (B) Representative analysis of HIFs by western blot: 50ug of protein from total cell lysate of blood leukocytes isolated from mice treated with PHZ compared to untreated. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28112274), licensed under a CC-BY licence.

Western Blot: Rabbit Polyclonal HIF-1 alpha Antibody - Analysis of HIF-1 alpha antibody on mouse liver nuclear extracts. Image from a verified customer review.

Improved survival and blood–brain barrier function post pneumococcal infection in mice by anti-HIF-1 alpha treatment using echinomycin. a Schematic depicting treatment protocol of mice infected with S. pneumoniae (D39). Mice were infected i.p., followed by anti-HIF-1 alpha treatment with echinomycin or just vehicle every 12 h starting 4 h post-infection (blue tick marks). Clinical scores were taken every 4 h starting 16 h post-infection (red line with tick marks) and study terminated at 48 h post-infection and brain tissues collected upon animal death or at the end point when the animals were sacrificed. b Clinical scores indicate improved symptoms in echinomycin-treated mice compared to vehicle-treated animals starting 16 h post-infection that were progression free (below score 1) up to 24 h (mean ± SEM at each time, N = 10/group, ****p < 0.0001, **p < 0.01, *p < 0.05 by 2-tailed unpaired non-parametric Mann–Whitney t test at each time point. c Echinomycin-treated mice showed significantly improved overall survival percentage by Kaplan–Meier analysis with the median survival at 32 h compared to 25 h in vehicle-treated mice (**p < 0.01, log-rank test, N = 10/group). d Kaplan–Meier analysis also indicated a significant improvement in progression-free survival in echinomycin-treated animals (median survival 25 h) with no clinical symptoms up to 24 h (b) compared to the vehicle group (median survival 17 h; ***p < 0.001, log-rank test, N = 10/group). e Immunofluorescence staining for HIF-1 alpha , BBB permeability and junctional markers in the echinomycin and vehicle groups at the survival end point. Left panel shows that echinomycin treatment leads to a reduction in HIF-1 alpha -positive nuclei including in ECs co-stained for podocalyxin, a vascular marker which was unchanged by the treatment. Middle panel displays reduced vascular permeability to fibrinogen in the echinomycin group as indicated by stronger intravascular signal compared to the vehicle-treated mice. Increased expression of tight junction proteins—occludin (middle panel) and claudin-5 (right top panel)—in echinomycin-treated mice indicate improved BBB function. Tight junction-associated ZO-1, adherens junction marker VE-Cadherin, and endothelial cell adhesion molecule CD31 were unchanged (middle, bottom right panel). There was also no difference in S. pneumoniae (Spn) staining (right top panel) between the two groups. Scale bar 10 μm. f Quantification of the staining from e utilizing four images per animal in the cortex region shows a significant reduction in HIF-1 alpha -positive cell number, whereas the total cell number or EC cell number was unchanged (left panel). As observed in e, the middle panel for quantification (arbitrary units—a.u.) of fibrinogen leakage shows significantly increased vascular staining for fibrinogen, supported by significantly increased expression of occludin, claudin-5, whereas other EC junction markers were unchanged. S. pneumoniae numbers in the vessels (v-Spn) or those transmigrated into brain parenchyma (b-Spn) were also unchanged. (mean ± SEM, N = 7–10/group indicated by the corresponding number of dots, ****p < 0.0001, **p < 0.01, *p < 0.05 by 2-tailed unpaired Student’s t test) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32529267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Compound MI-743 causes intracellular 8-oxo-dG accumulation and DNA damage.a MGC-803, HGC-27 and GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 and GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h and run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15 in MGC-803, HGC-27 and GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 and 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15 of protein lysates, isolated from MGC-803, HGC-27 and GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 and 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Successful knockdown of HIF-2 alpha in both 786-O and A498 renal cell lines. (A) Lysates from 786-O cells stably transfected with VHL (VHL +), parental 786-O cells (786-O), and 786-O cells infected with an empty retrovirus (pSuperRetro) or with retroviruses encoding single HIF-2 alpha shRNAs (HIF2 alpha shRNA 1; HIF2 alpha shRNA 2) or doubly infected with both shRNAs (HIF2 alpha shRNA 1+2) were immunoblotted for HIF-2 alpha (top panel), GLUT1 (upper middle panel) and VHL (lower middle panel). Bottom panel is an alpha tubulin immunoblot to demonstrate equal protein loading (25 μg) in each lane. (B) Lysates from A498 cells stably transfected with VHL (VHL +), parental A498 cells (A498), and A498 cells infected with an empty retrovirus (pSuperRetro) or doubly infected with both HIF-2 alpha shRNAs (HIF2 alpha shRNA 1+2) were immunoblotted as in (A). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/17598890), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

IQGAP1 induces the epithelial-to-mesenchymal transition, invasiveness, and proliferation of endometrial cancer (EC) cellsA. Reverse transcription quantitative PCR (qPCR) analysis of IQGAP1 mRNA in the immortalized human endometrial cell line EM and the EC cells HEC-1, HEC-50, and HEC-50-HI (HI). The results are presented as the fold-change in expression compared to the EM cells. B. Western blot analysis of the IQGAP1 protein in EC cells. C, E. The expression of IQGAP1, E-cadherin, and N-cadherin proteins in HI cells transfected with control (Ctr) or IQGAP1 siRNA (C) and in HEC-1 cells expressing either the control or IQGAP1 vector (E). D, F. Phase-contrast microscopy shows the morphology of HI cells transfected with control or IQGAP1 siRNA (D) and HEC-1 cells transfected with the control or IQGAP1 vector (F). G-I. Detection of migration (G), invasion (H), and proliferation (I) in HI and HEC-1 cells after the indicated transfection. J, K. qPCR analysis of ZO-1, CK-18, and Vimentin expression in HI (J) and HEC-1 (K) cells, transfected as indicated. L. Representative images from the invasion assays. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.7754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

FDFT1 inhibits glycolysis through suppressing the AKT-mTOR-HIF1 alpha pathway in CRC.aFDFT1 overexpression reduced glucose uptake in CT26 cells. bFDFT1 overexpression decreased lactate production via glycolysis in CT26 cells. c ECAR was reduced when FDFT1 was overexpressed in CT26 cells. d OCR was increased when FDFT1 was overexpressed in CT26 cells. eFDFT1 knockdown increased glucose uptake in CT26 cells. fFDFT1 knockdown increased lactate production via glycolysis in CT26 cells. g ECAR was increased when FDFT1 was knocked down in CT26 cells. h OCR was decreased when FDFT1 was knocked down in CT26 cells. i, mFDFT1 overexpression inhibited the protein and mRNA expression of mTOR-targeted glycolytic enzymes, including GLUT1, HK2, PGK1, GPI, and LDHA, in CT26 cells. j, mFDFT1 knockdown increased the protein and mRNA expression of mTOR-targeted glycolytic enzymes, including GLUT1, HK2, PGK1, GPI, and LDHA, in CT26 cells. k, nFDFT1 overexpression decreased the protein and mRNA expression of AKT, mTOR, and HIF1 alpha . l, nFDFT1 knockdown increased the protein and mRNA expression of AKT, mTOR, and HIF1 alpha . o Photograph of dissected tumors (the first line: normal diet, the second line: FMD + glucose, the third line: FMD, n = 5). p The tumor volumes were measured every 2 days after the 13th day. The FMD + glucose group can reverse the tumor growth inhibition induced by the FMD (n = 5; ns: P = 0.1838; P = 0.0001). q The protein level of FDFT1 and mTOR in dissected tumor samples from normal diet group, FMD group and FMD + glucose group was measured by western blotting. r The glucose level in these three groups. Error bars, mean ± SD, the data are from three independent experiments. Two-sided t tests. *P < 0.05, **P < 0.01, ***P < 0.001, compared with the control group (or normal diet group). #P < 0.05, ##P < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32313017), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effect of MLL-HCF1 interaction on histone methylation and Nrf2 expression in SNUC5/5-FUR cellsA. HCF1 expression was determined by Western blotting. *Significantly different from SNUC5 cells (p<0.05). B. Interaction between MLL and HCF1was examined by immunoprecipitation analysis using anti-MLL and anti-HCF1 antibodies followed by Western blotting with anti-HCF1 and anti-MLL antibodies. *Significantly different from SNUC5 cells (p<0.05). C. Interaction between MLL and HCF1was assessed by PLA. Each green spot represents for a single interaction (MLL and HCF1) and DNA was stained with DAPI. *Significantly different from SNUC5 cells (p<0.05). The cells were transfected with non-targeting siRNA (siControl) or siHCF1 RNA for 24 h. D. Expression pattern of MLL mRNA in SNUC5/5-FUR cells was determined by RT-PCR analysis. *Significantly different from siControl-transfected cells (p<0.05). E. Expression pattern of HCF1, MLL, and Nrf2 in SNUC5/5-FUR cells was determined by Western blot analysis. *Significantly different from siControl-transfected cells (p<0.05). Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.9745), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Induction of ubiquitin/proteasome-dependent DSBs in CPT-treated quiescent WI38 hTERT cells. (A–F) Serum-starved cells were treated with DMSO (1 h) or with MG132 (50 μM, 1 h), lactacystin (10 μM, 1 h), bortezomib (1 μM, 4 h), G5 (1.5 μM, 0.5 h) or Pyr-41 (9 μM, 0.5 h) before the addition of DMSO (untreated) or 25 μM CPT for 1 h and then co-stained for gamma H2AX (green) and 53BP1 (red) or analyzed by Western blot. ‘-’ in panels C and F means cells treated with DMSO. (A and D) Representative pictures. Nuclear contours, identified by DAPI staining (not shown), are indicated by dashed lines. Bars: 10 μm. (B and E) Number of gamma H2AX foci per nucleus from two independent experiments (147–153 nuclei were analyzed for each treatment). ****P < 0.0001. (C and F) Western blot of gamma H2AX. alpha Tubulin: loading control. Dashed lines indicate that intervening wells have been spliced out. The top panels show quantification of gamma H2AX normalized to alpha Tubulin (means ± SEM, n = 4 in panel C, n = 3 in panel F). ***P < 0.001; **P < 0.01. (G and H) Detection of DSBs by neutral Comet assays in serum-starved cells treated with DMSO or MG132 (25 μM) for 1 h before the addition of DMSO (untreated) or CPT for 1 h (7.5 μM for experiments (Exp) I and II; 5 and 7.5 μM for Exp III). (G) Representative pictures of nuclei from Exp I. (H) Quantification of neutral Comet tail moments for three independent experiments (95–133 nuclei were analyzed for each treatment in each experiment). ***P < 0.001; ****P < 0.0001. The untreated and CPT data from Exp I are from the same experiment as that of Supplementary Figure S3D. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26578593), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$S100A7 is secreted and acts as a chemotactic factor of cell migration and invasionA. Cells were cultured in serum-free medium for 2 days, then the medium was collected, fractioned, followed by Western Blot analysis. B&C. Transwell migration and Matrigel invasion assays were performed in C33A and SiHa cells. Cell suspension was placed into the upper chamber in 0.1 ml of DMEM serum-free medium, and conditioned medium from S100A7-overexpressed C33A and SiHa cells and their corresponding control cells was placed in the lower chamber as a chemoattractant. The stained cells were manually counted from 4 randomly selected fields and normalized with cell proliferation [2-sided t test; *P < 0.05; ***P < 0.001]. Representative image and quantitative results of cell migration and invasion were shown (B. C33A cells; C. SiHa cells; ×10, bars:100μm). Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15329), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Increased expression of HIF alpha and/or Twist in A549 and H441 cells induced by the inhibition of PIMT and Thapsigargin(A) Immunoblotting of Slug, ZEB1, Snail1, Twist, and HIF1 alpha in A549 sh-PIMT and sh-control cells. (B, C) Immunoblotting and relative intensity of HIF1 alpha in A549 cells treated with Tg. (D) Immunoblotting of Slug, ZEB1, Snail1, Twist, and HIF1 alpha in si-control cells and si-PIMT H441 cells. (E, F) Immunoblotting and relative intensity of HIF1 alpha in H441 cells treated with Tg. #1 and #2 indicates si-RNA of J-010000-05-0002 and J-010000-07-0002, respectively. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.24324), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Characterization of CIP2A expression in a panel of normal human melanocytes (NHM) and melanoma cell lines. (A) Immunoblot analysis and (B) quantification of protein expression levels of CIP2A (C) CIP2A mRNA expression measured by qRT-PCR. NHM1 line was used as calibrator. (D) Cytoplasmic and nuclear expression of CIP2A in normal melanocytes, primary and metastatic melanoma cell lines assessed by immunoblot analysis and (E) by immunohistochemical staining. CIP2A, cancerous inhibitor of protein phosphatase 2A. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25663244), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Role of inflammasome in glucose fluctuation-induced myocardial fibrosis. (A) Immunofluorescence staining of intracellular NLRP3–ASC interaction examined by confocal microscopy. The NRCFs were labeled with anti-NLRP3 (red), anti-ASC (green), and DAPI (blue) (n = 3 per group). (B–G) After siRNA targeting NLRP3 transfection, the protein expressions of NLRP3, cleaved caspase-1 and collagen I were measured by western blot (n = 3 per group). (H) Representative images of immunofluorescence staining of intracellular alpha -SMA in the NG, HG, GF, and GF + siRNA groups (n = 3 per group). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Ch, Gt, Pm, Pm, Bv

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Ch, Gt, Pm, Pm, Bv

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

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NBP2-75977

HIF-1 alpha Antibody (2443B) - BSA Free

0.1 mg

NBP2-75977

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (2443B) [NBP2-75977] - Immunofluorescent staining of HIF-1 alpha using catalog number NBP2-75977 (clone 2443B). Staining was observed in Hela cells treated with DFO but not in untreated Hela cells.

Simple Western: HIF-1 alpha Antibody (2443B) [NBP2-75977] - Lane view shows a specific band for HIF-1 alpha in HepG2 +/- DFO cell lysate using 20ug/ml. Electropherogram image of corresponding Simple Western lane view at WES molecular weight of 116 KDa. Image from an internal validation.

Simple Western: HIF-1 alpha Antibody (2443B) [NBP2-75977] - Simple Western lane view shows lysates of MCF +/- DMOG, BioSpherix MSCs in hypoxic conditions, and BioSpherix MSCs in normoxic conditions loaded at 0.5 mg/ml. A band was detected for HIF-1 alpha at approximately 116 kDa (as indicated) using NBP2-75977 (1:100 dilution) followed by Anti-Rabbit Secondary Antibody (042-206, ProteinSimple). This experiment was conducted under standard assay conditions, and using the 12-230 kDa separation module (SW-W004). Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody. Image from an internal validation.

Reactivity:

Hu

Species Glossary

Reactivity: Hu

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Monoclonal

Host: Rabbit Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-75977AF350
Alexa Fluor 405	NBP2-75977AF405
Alexa Fluor 488	NBP2-75977AF488
Alexa Fluor 532	NBP2-75977AF532
Alexa Fluor 594	NBP2-75977AF594
Alexa Fluor 647	NBP2-75977AF647
Alexa Fluor 700	NBP2-75977AF700
Alexa Fluor 750	NBP2-75977AF750
Allophycocyanin	NBP2-75977APC
Biotin	NBP2-75977B
DyLight 350	NBP2-75977UV
DyLight 405	NBP2-75977V
DyLight 488	NBP2-75977G
DyLight 550	NBP2-75977R
DyLight 594	NBP2-75977DL594
DyLight 650	NBP2-75977C
DyLight 680	NBP2-75977FR
DyLight 755	NBP2-75977IR
FITC	NBP2-75977F
HRP	NBP2-75977H
Janelia Fluor 549	NBP2-75977JF549
Janelia Fluor 646	NBP2-75977JF646
PE	NBP2-75977PE
PerCP	NBP2-75977PCP
mFluor Violet 450 SE	NBP2-75977MFV450
mFluor Violet 500 SE	NBP2-75977MFV500
mFluor Violet 610 SE	NBP2-75977MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-75977SS
Azide and BSA Free	NBP2-80764

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NBP2-75978

HIF-1 alpha Antibody (2443C) - BSA Free

(2 Reviews)

(1 Publication)

0.1 mg

NBP2-75978

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (2443C) [NBP2-75978] - Immunofluorescent staining of HIF-1 alpha using catalog number NBP2-75977 (clone 2443B). Staining was observed in Hela cells treated with DFO but not in untreated Hela cells.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (2443C) [NBP2-75978] - HIF-1 alpha (clone 2443C) was detected in immersion fixed paraffin-embedded sections of human kidney using Rabbit Anti-Human HIF-1 alpha Monoclonal Antibody (Catalog # NBP2-75978) at 1.0 ug/mL for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte (TM) HRP Polymer Antibody (Catalog # VC002). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the nuclei.

Simple Western: HIF-1 alpha Antibody (2443C) [NBP2-75978] - Lane view shows a specific band for HIF-1 alpha in HepG2 +/- DFO cell lysate using 20 ug/mL. Electropherogram image of corresponding Simple Western lane view at WES molecular weight of 116 KDa. Image from an internal validation.

Simple Western: HIF-1 alpha Antibody (2443C) [NBP2-75978] - Simple Western lane view shows lysates of MCF +/- DMOG, BioSpherix MSCs in hypoxic conditions, and BioSpherix MSCs in normoxic conditions loaded at 0.5 mg/ml. A band was detected for HIF-1 alpha at approximately 116 kDa (as indicated) using NBP2-75978 (1:100 dilution) followed by Anti-Rabbit Secondary Antibody (042-206, ProteinSimple). This experiment was conducted under standard assay conditions, and using the 12-230 kDa separation module (SW-W004). Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody. Image from an internal validation.

Reactivity:

Hu

Species Glossary

Reactivity: Hu

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Monoclonal

Host: Rabbit Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-75978AF350
Alexa Fluor 405	NBP2-75978AF405
Alexa Fluor 488	NBP2-75978AF488
Alexa Fluor 532	NBP2-75978AF532
Alexa Fluor 594	NBP2-75978AF594
Alexa Fluor 647	NBP2-75978AF647
Alexa Fluor 700	NBP2-75978AF700
Alexa Fluor 750	NBP2-75978AF750
Allophycocyanin	NBP2-75978APC
Biotin	NBP2-75978B
DyLight 350	NBP2-75978UV
DyLight 405	NBP2-75978V
DyLight 488	NBP2-75978G
DyLight 550	NBP2-75978R
DyLight 594	NBP2-75978DL594
DyLight 650	NBP2-75978C
DyLight 680	NBP2-75978FR
DyLight 755	NBP2-75978IR
FITC	NBP2-75978F
HRP	NBP2-75978H
Janelia Fluor 549	NBP2-75978JF549
Janelia Fluor 646	NBP2-75978JF646
PE	NBP2-75978PE
PerCP	NBP2-75978PCP
mFluor Violet 450 SE	NBP2-75978MFV450
mFluor Violet 500 SE	NBP2-75978MFV500
mFluor Violet 610 SE	NBP2-75978MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-75978SS
Azide and BSA Free	NBP2-80765

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NB100-134

HIF-1 alpha Antibody - BSA Free

(14 Reviews)

(220 Publications)

0.1 ml

NB100-134

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody - BSA Free [NB100-134] - Analysis of HIF-1 alpha in zebrafish retina tissue using NB100-134 HIF-1 alpha antibody. Mouse tissue was used as a control. Image from verified customer review.

Western Blot: HIF-1 alpha Antibody - BSA Free [NB100-134] - Analysis of HIF-1 alpha in overexpression and endogenous HIF-1 alpha & HIF-2 alpha using anti-HIF-1 alpha antibody NB100-134. The data showed that HIF-1 alpha antibody did not react to HIF-2 alpha overexpression. Image from verified customer review.

Western Blot: HIF-1 alpha Antibody - BSA Free [NB100-134] - Analysis of HIF-1 alpha using NB100-134, on normoxic and hypoxic nuclear rat cell lysates.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody - BSA Free [NB100-134] - Representative images of macrophages and activated macrophages, in the absence or presence of 10 uM hemin for 72 h. HIF-1 alpha levels were detected by immunofluorescence using a confocal imaging system (Opera Phenix, Perkin Elmer). Images were acquired with 20x water objective. Staining intensity levels in the nucleus and cytosolic region were obtained using Harmony software (Perkin Elmer). Nucleus and cytosol were identified through Hoechst (at 405 nm) and CellMask (at 655 nm) staining, respectively. Scale is shown as 100 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33187129/) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody - BSA Free [NB100-134] - Analysis of HIF-1 alpha in Normoxic (N) and Hypoxic (H) ARPE-19 cells using anti-HIF-1 alpha antibody NB100-134. Image from verified customer review.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody - BSA Free [NB100-134] - Hif1alpha expression in 9.5dpc primordial germ cells. Whole-mount staining of Hif1alpha and GFP in Oct4-GFP embryo (lateral view). Scale bar: 100um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0154309) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody - BSA Free [NB100-134] - Staining in the canine CL on days 10 to 70 after ovulation. PC = positive control (human placenta). NC = negative control. Image from verified customer review.

Immunohistochemistry: HIF-1 alpha Antibody - BSA Free [NB100-134] - Staining of human kidney, renal tubular epithelium in cortex using NB100-134.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody - BSA Free [NB100-134] - Analysis of FFPE tissue section of human endometrium carcinoma AN3CA cell line based xenograft using rabbit polyclonal HIF-1 alpha antibody NB100-134 at 1:300 dilution. The signal was developed using HRP-labelled secondary antibody and DAB reagent, and the section was further counterstained using hematoxylin. The tested section depicted mainly a diffused cytoplasmic staining but there were some cells which showed nuclear signal also (representing hypoxic cells).

Simple Western: HIF-1 alpha Antibody - BSA Free [NB100-134] - Image shows a specific band for HIF-1 alpha in 0.2 mg/mL of Hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Immunoprecipitation: HIF-1 alpha Antibody - BSA Free [NB100-134] - PC-3 cell lysates run with cobalt chloride treatments. Immunoprecipitation was performed with protein A/G agarose beads. This data was provided courtesy of Kelie Reece, Figg lab, NCI.

Dual RNAscope ISH-IHC: HIF-1 alpha Antibody - BSA Free [NB100-134] - Formalin-fixed paraffin-embedded tissue sections of human kidney were probed for HIF-1 alpha mRNA (ACD RNAScope Probe, catalog #605228; Fast Red chromogen, ACD catalog # 322750). Adjacent tissue section was processed for immunohistochemistry using Rabbit Polyclonal (Novus Biologicals catalog # NB100-134) at 1:500 dilution with one-hour incubation at room temperature followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody (Catalog # VC003) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm of tubules.

Simple Western: HIF-1 alpha Antibody - BSA Free [NB100-134] - Simple Western lane view shows lysates of MCF +/- DMOG, BioSpherix MSCs in hypoxic conditions, and BioSpherix MSCs in normoxic conditions loaded at 0.5 mg/ml. A band was detected for HIF-1 alpha at approximately 116 kDa (as indicated) using NB100-134 (1:100 dilution) followed by Anti-Rabbit Secondary Antibody (042-206, ProteinSimple). This experiment was conducted under standard assay conditions, and using the 12-230 kDa separation module (SW-W004). Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody. Image from an internal validation.

P53 was increased response to IR in the fetal brain.Even though no significant change in protein level, total p53 and phosphorylation of P53 at ser15 were increased compared with HIF-1 alpha in fetal brains response to IR. Numbers in the pictures show the average of three independent experiments (n = 3 from 3 individual pregnant mice).

IGFBP5 inhibits HIF1alpha expression through the MAPK-ERK signaling pathway. C). Overexpression of IGFBP5 inhibited HIF1alpha expression visualized by western blots of A375 cells. The arrow points to the band of HIF1alpha. D. Assessment of the reduced gene expression levels of VEGFA and MMP9, downstream genes regulated by HIF1alpha, in A375 IGFBP5 OE compared to control cells by qRT-PCR analysis. Data were shown for the mean +/- SD form three independent experiments. P values based on two-side Student t-test comparing A375 IGFBP5 OE tumor cells and vector control cells. *, P 25 pictures/group from three separate experiments. Scale bar = 40 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31083380), licensed under a CC-BY licence.

ER-INP binds to PHD2, inhibits hydroxylation of HIF-1alpha and increases HIF-1alpha accumulation. (B) Western blot analysis to measure the effect of ER-INP on HIF-1alpha and its hydroxylation level in transfected HEK293 and RAW264.7 cells pre-treated with MG132 (upper panel) and the protein ratio to beta-actin loading control by ImageJ densitometry analysis (lower panel; n = 3). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31413262), licensed under a CC-BY licence.

HIF-1alpha levels are increased by androgen stimulus and Tip60 overexpression in LNCaP cells. (A) Nuclear and (B) cytosolic HIF-1alpha levels and (C) images in LNCaP cells and in LNCaP cells overexpressing Tip60, in the absence or presence of androgen (10 nM R1881, 72 h). HIF-1alpha levels were detected by immunofluorescence using confocal imaging system. Images were acquired with 20x objective. Staining intensity levels in the nucleus and cytosolic region were obtained using Harmony software. Nucleus and cytosol were identified through Hoechst and CellMask staining, respectively. Scale is shown as 100 um. White dotted frames indicate the section of the image that was enlarged. Values are expressed as mean +/- SEM, from three independent culture preparations, each treatment performed in quadruplicate. Two-way ANOVA, Bonferroni post-test and p values comparisons are specified in the figures (* p < 0.05). HIF-1alpha, hypoxia-inducible factor-1alpha; OE, overexpressing; R1881, synthetic androgen. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31671779), licensed under a CC-BY licence.

The increase of cytosolic HIF-1alpha levels of activated macrophages is inhibited by hemin. (C) Representative images of macrophages and activated macrophages, in the absence or presence of 10 uM hemin for 72 h. HIF-1alpha levels were detected by immunofluorescence using a confocal imaging system (Opera Phenix, Perkin Elmer). Images were acquired with 20x water objective. Staining intensity levels in the nucleus and cytosolic region were obtained using Harmony software (Perkin Elmer). Nucleus and cytosol were identified through Hoechst (at 405 nm) and CellMask (at 655 nm) staining, respectively. Scale is shown as 100 um. White dotted frames indicate the section of the image that was enlarged. Values with different superscript letters (a and b) indicate significant differences (p < 0.05) between groups. For all bars with the same letter, the difference between the means is not statistically significant. HIF-1alpha, hypoxia-inducible factor-1 alpha. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33187129), licensed under a CC-BY licence.

LOXL2 abundance in EC-derived exosomes is increased in hypoxia. (A) Immunoblots of endothelial cells for HIF-1alpha (control for hypoxia, top panel), LOXL2 (middle panel) and beta-actin (loading control, lower panel). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26612622), licensed under a CC-BY licence.

Hypoxic setup for larval zebrafish. (D) Western blot of Hif1alpha protein expression showing that hypoxia enhanced Mbp protein translation. *P < 0.05; **P < 0.01; ***P < 0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30337858), licensed under a CC-BY licence.

Enhanced expression of hypoxia-induced survival factors and angiogenic growth factors in hASC L-spheroids. (C) Western blot analysis and quantification of HIF1-alpha in hASCs cultured as spheroids, L-spheroids and monolayers (*p < 0.01, compared to the L-spheroid group). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26065900), licensed under a CC-BY licence.

E2 enhances neutrophil apoptosis through suppressing the expression of hif1alpha and c-myb under physiological conditions. C) Staining of hif1alpha with antibody with or without E2 treatment. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35842445), licensed under a CC-BY licence.

HIF1alpha and AhR mediate butyrate induction of IL-22 in CD4+ T cells.. b-f CD4+ T cells were activated with anti-CD3/CD28 mAbs +/- butyrate (0.5 mM) under Th1 conditions (n = 3/group). Hif1a (b) and Ahr (c) were analyzed by qRT-PCR. HIF1alpha (d) and AhR (e) protein was analyzed by western blot on day 2. HIF1alpha activity was measured using HIF1alpha Transcription Factor Assay Kit (f). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32901017), licensed under a CC-BY licence.

$Alteration of PARKIN leads to an impairment of mitophagy upon CCCP treatment.a 2 N and DS were treated with CCCP (20 μM) for 6 h and mitochondrion/cytosol fractionation was performed to assay the accumulation of LC3-II and p62 within the mitochondrial fraction. VDAC1 and ACTIN were used as a loading control for mitochondrial and cytosolic fractions, respectively. b, c Quantitative data of LC3-II and p62 in the mitochondrial fraction were normalized with VDAC1 (n = 3). d The cells were treated with CCCP (20 μM) for 6 h and the whole-cell extracts from 2 N and DS were analyzed by western blot for PARKIN and PINK1. e Quantification of PARKIN normalized with ACTIN (n ≥ 3). d Quantification of PINK1 after 6 h of CCCP, each quantitative data was normalized with ACTIN (n ≥ 3). g Representative confocal images of cells stained with Mitotracker green (mitochondrial marker) and Lysotracker red (lysosomal marker) upon CCCP treatment (20 μM for 6 h). White arrow heads point to the co-localization within puncta from the boxed region at high magnification shown on the right. Scale bar 10 μm. h The graph shows the percentage of Mitotracker green /Lysotracker red colocalization calculated by JACoP plugin of ImageJ. Minimum 50 cells per condition were counted from three independent experiments. i 2 N and DS cells were treated with CCCP (20 μM) for 6 h and were assessed for SQSTM1 (p62), PARKIN and PINK1 mRNA by quantitative real-time PCR. mRNA levels were normalized to ACTIN mRNA, used as internal control. Data display the fold-changes of SQSTM1, PARKIN and PINK1 mRNAs relative to control cells (n = 3). Statistical analysis was performed using Student’s T-test or one-way ANOVA with Tukey’s multiple comparisons test. (*p < 0.05; **p < 0.01; ***p < 0.001; n.s. no significant difference). Immunoblots reported are from one representative experiment Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31332166), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

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

Metformin synergized with sorafenib to suppress angiogenesis, proliferation, and EMT but promote apoptosis in vivo. Representative images of tumor sections were stained with antibody against CD31, Ki67, and TUNEL (magnification ×200). a Metformin in combination with sorafenib synergistically minimized both Ki67 and CD31 expression but promoted TUNEL expression. b Combined therapy inhibited EMT at protein level which lysated from the tumor tissue, and pAMPK expression was elevated both in metformin group and combined treatment groups. c Combined treatment of metformin and sorafenib suppressed HIF-2 alpha protein expression but upregulated TIP30 protein expression evaluated by Western blot Image collected and cropped by CiteAb from the following open publication (//www.jhoonline.org/content/9/1/20), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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

Impacts of PRDX3 protein on autophagy flux(A–D) Representative immunoblot (A, C) and quantification (B, D) showing the levels of LC3-II in BPH-1 cells treated with random (MOCK) or PRDX3-specific siRNA (PRDX3) (A, B) or RWPE-1 cells transiently expressing different amount of PRDX3 (C, D) in the absence (Ctrl) or presence of bafilomycin A1 (BAF). Data are mean and standard deviation of three repeats and differences are tested with Student's T-test. *P ≤ 0.05; **P ≤ 0.01; ***P ≤ 0.001. (E–G) Representative immunoblot (E) and quantification (F, G) showing the levels of Beclin 1 (F) and PI3KCIII (G) in BPH-1 cells treated with random (MOCK) or PRDX3-specific siRNA (PRDX3). Ns, not significant; *P ≤ 0.05. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.17927), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Autophagy level was promoted by downregulation of the Hh signaling pathway in zebrafish larvae. (A–C) Larvae were exposed to 10 µM cyA and 0.1% DMSO at 3 dpf for 3 days. (D–H) Embryos were injected with SHHMO, Gli2MO and Gli2Mis at the 1–4 cell stage; at 6 dpf, larvae were collected for assays . GAPDH served as a loading control. The means and s.d. were derived from triple duplicates. *P<0.05, **P<0.01, ***P<0.001 versus the WT groups or DMSO control groups (one-way ANOVA). The data were from three independent experiments. (A,D) SHH protein was detected by western blot assay. (B,E,G) Transcriptional level of autophagy-related genes was tested by qPCR assays. (C,F,H) Autophagy-related proteins LC3B II, ATG5 and P62 level were determined by western blot. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30992325), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

FASN Regulates HIF-alpha Protein Stability and HIF Target Gene Expression. (A) FASN siRNA downregulates HIF-alpha protein levels. PREC, HeLa and HCT116 cells were treated with FASN (+) or control (−) siRNA and harvested after 72 h. Cells were exposed to hypoxia (1% oxygen) or maintained in normoxia (21% oxygen) 4 h before harvesting and subjecting WCEs to western blot analysis. Unmodified (250 kDa) and modified (larger) FASN bands are indicated by large arrowheads, REDD1 by a small arrowhead, and HIF-1 alpha and HIF-2 alpha by arrows. (B) Downregulation of HIF-1 alpha and HIF-2 alpha in HCT116 cell clones carrying the FASN gene mutagenized using CRISPR-Cas9 (See Supplementary Fig. S3 for genomic DNA information). Protein samples were prepared in normoxia (left column) or hypoxia (right column) for western blot analysis. Asterisk indicates a non-specific band. (C) Quantification of HIF-target gene expression by qPCR upon downregulation of FASN in PREC. Samples were prepared from cells treated as described for panel A but with 24 h hypoxia. siRNAs were transfected in triplicates and mRNAs of the HIF target genes were measured in biological triplicates and technical duplicates as a total of 6 samples by qPCR. Values were normalized against the PPIA reference gene and control samples. (D) Loss of downregulation of HIF-2 alpha levels in ccRCC cells. pVHL-deficient 786-O and A498 cells were tested in FASN siRNA knockdown experiments. (E) Restoration of HIF-alpha regulation by stable expression of exogenous pVHL in SKRC10 cells. pVHL-WT or pVHL-Y112H were introduced into pVHL-deficient SKRC10 ccRCCs using a lentiviral vector carrying a weak promoter and HIF-alpha protein levels were examined. Specific and non-specific bands are indicated by arrows and an asterisk, respectively. (F) FASN and the E3 ligase components are present in the pVHL-containing complexes in a mutually exclusive manner. The indicated constructs were transfected into 293 T cells and WCEs prepared after 48 h were tested for protein-protein interactions by precipitation with an anti-Flag antibody-conjugated resin. Note that FASN failed to precipitate CUL2 and Elongin C, as shown in lanes 6 and 8. Experiments were repeated twice (D,E,F) or more (A,B), and the results were reproduced. The qPCR experiment (C) was performed once with biological triplicates. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28775317), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Etv5b activates the smn promoter leading to increased Smn levels in motoneurons.(a–d) Whole-mount in situ hybridization of etv5b expression in 24 hpf embryos. Expression pattern in the entire embryo (a), in magnified lateral (b) and dorsal (c) views as well as in a transverse section (d) of the trunk. In the latter case, yellow arrowhead denote signal in the motoneuron region. Scale bars: 100 μm (a) and 50 μm (b–d). nc, notochord. (e) RT-PCR in control (C - only psmn:mCherry) versus etv5b overexpressing (OE - etv5b mRNA and psmn:mCherry) embryos at early gastrula stage. (f,g) scIF of control (f) and etv5b MO (g) cells from pmnx1:eGFP embryos. H2B, GFP and Smn signals are shown in Z-projected confocal sections. GFP+ cells marked by white rectangles are magnified on the right. Scale bars: 10 μm for low and 5 μm for high magnification. (h) Relative Smn signal in control and in etv5b MO cells from one representative experiment. Exact values are (mean ± SD): 0.99 ± 0.25 (control) and 0.7 ± 0.14 (etvb5 MO), p = 0.003 with Wilcoxon Sum Rank Test. (i) Average relative Smn levels in control and in etv5b MO motoneurons. The exact value of decrease is 0.75 ± 0.04 (mean ± SD). N = 3 experiments, n = number of analyzed cells. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep27470), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The A2AR and baicalin attenuated CXCR4 expression in the hypoxia-induced PAH mouse model. CXCR4 and MYH11 expression levels in mouse PASMCs were analyzed by immunofluorescence staining (a; n = 3). CXCR4 protein is stained red, and MYH11 is stained green to indicate the PASMCs (×400; scale bars indicate 50 μm). CXCR4 fluorescence intensity was calculated (b; n = 3). CXCR4 protein expression levels in lung tissue were examined by western blot. GAPDH served as an internal control (c, d; n = 3). Data are presented as the mean ± SD. #Value significantly greater than the corresponding value in saline-treated normoxic mice (##P < 0.01). *Value significantly less than the corresponding value in hypoxic mice (*P < 0.05, **P < 0.01). §Value significantly less than the corresponding value in baicalin-treated mice (§P < 0.05, §§P < 0.01). +Value significantly different between WT and A2AR−/− mice (+P < 0.05, ++P < 0.01). WTH, wild-type hypoxic; A2AR−/−H, A2AR−/− hypoxic; s, saline-treated Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28774332), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Bv, Ca, Gp, Pm, Xp, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Bv, Ca, Gp, Pm, Xp, Ze

Applications:

, , , , , , , , , ,

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

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-134AF350
Alexa Fluor 405	NB100-134AF405
Alexa Fluor 488	NB100-134AF488
Alexa Fluor 532	NB100-134AF532
Alexa Fluor 594	NB100-134AF594
Alexa Fluor 647	NB100-134AF647
Alexa Fluor 700	NB100-134AF700
Alexa Fluor 750	NB100-134AF750
Allophycocyanin	NB100-134APC
Biotin	NB100-134B
DyLight 350	NB100-134UV
DyLight 405	NB100-134V
DyLight 488	NB100-134G
DyLight 550	NB100-134R
DyLight 594	NB100-134DL594
DyLight 650	NB100-134C
DyLight 680	NB100-134FR
DyLight 755	NB100-134IR
FITC	NB100-134F
HRP	NB100-134H
Janelia Fluor 549	NB100-134JF549
Janelia Fluor 646	NB100-134JF646
PE	NB100-134PE
PerCP	NB100-134PCP
mFluor Violet 450 SE	NB100-134MFV450
mFluor Violet 500 SE	NB100-134MFV500
mFluor Violet 610 SE	NB100-134MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-134SS

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NBP2-12446

NLRP3/NALP3 Antibody - BSA Free

(4 Reviews)

(223 Publications)

0.2 ml

NBP2-12446

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

Hu, Mu, Rt, RM

Species Glossary

Reactivity: Hu, Mu, Rt, RM

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-6668A

Alt Catalog# IMG-6668A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-12446SS

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NB100-123

HIF-1 alpha Antibody (H1alpha67)

(9 Reviews)

(157 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.

Dapagliflozin protects against metabolic switch by inhibition of HIF-1alpha. b Representative images of PTCs incubated with 10 umol/l of molidustat for 6 h with immunofluorescent staining for HIF-1alpha. Scale bar = 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32444604), licensed under a CC-BY licence.

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), and the levels of hypoxia-inducible factor HIF1alpha (C) in orthotopic tumor xenografts. Scale bar: Montage, 1 mm; 10X, 20 um. 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 and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30723259), licensed under a CC-BY licence.

Analysis of CBF treatment in HCT116 implanted mouse models and tumour tissue samples. (c) Inhibition of HIF-1alpha nuclear translocation in the i.t. sample. CBF strongly inhibited HIF-1alpha nuclear accumulation in the tumour of xenografts implanted with HCT116 cells. Scale bars equal 10 um. White arrows: HIF-1alpha in the cytosol. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23818933), licensed under a CC-BY licence.

Analysis of single strand break repair in MCF-7 monolayer and mammosphere cell populations. (a) Cells were exposed to 4 Gy 60Co gamma -radiation and the relative degree of single-strand breakage (SSB) was determined by alkaline single-cell gel electrophoresis (comet assay) immediately after exposure and at the times indicated after exposure. (b) The 'comets' (n of about 100) were categorized according to the NIH LISTSERV (Comet Assay Interest Group web site) in which type 1 comets display the least DNA damage and type 5 the most. The error bars represent the mean ± standard error of the mean in both panels. The comets of the unirradiated cells are labeled Cont. (c) Expression of proteins involved in SSB repair in response to ionizing radiation. Lysates were prepared from unirradiated cells and from cells harvested one hour after exposure to 1 or 10-Gy 60Co gamma -radiation and analyzed by immunoblotting with antibodies against several SSB repair proteins. alpha -Actin served as a loading control. Image collected and cropped by CiteAb from the following open publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr2583), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

MTH1 suppression reduces the two gastric cancer cell survival.MGC-803, HGC-27 and GES-1 cells were treated by MTH1 specific siRNA#1 and #2 for 72 h. Non-targeting siRNA(NT) treatment was used as control. a Levels of MTH1 protein then were determined by western blot. b The colony formations were recorded after the cells were treated with MTH1 siRNA#1 and #2 for 7 days. c Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15, after the cells were treated with siRNA#2. f–h Densitometry shows relative protein expression normalized by GAPDH. d The Alkaline comets assay was performed after the cells were transfected with MTH1 siRNA#2 for 72 h. Pictures were originally captured at ×40 magnification by fluorescence microscope. Non-targeting siRNA(NT) or H2O2 treatment was used as a negative or a positive control, respectively. e Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. i Relative cell viability was determined by MTT assay, after the cells were treated with MTH1 siRNA#1 and #2 with or without MI-743 combined with 100uM H2O2. Data are presented as means ± SD. Three individual experiments were performed for each group. The symbols * and #, ** and ## or ***and ### stand for P < 0.05, P < 0.01 or P < 0.001 compared with the controls Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

SNX9 colocalizes with FCHSD1 in the cuticular plate of mouse cochlear hair cells.Shown are single confocal sections. SNX9 immunoreactivity visualized with FITC-conjugated secondary antibody was distinctly associated with the cuticular plate, which was visualized with rhodamine-conjugated phalloidin. (A) SNX9 immunoreactivity in the cuticular plate of 2-week old mouse cochlear hair cells. (B) SNX9 immunoreactivity in the cuticular plate of 3-week old mouse outer hair cells. (C) and (D) SNX9 immunoreactivity colocalized with FCHSD1 immunoreactivity, which was visualized with Cy5-conjugated secondary antibody, in the cuticular plate of 3 week-old mouse cochlear hair cells. The Novus FCHSD1 antibody was used in (C) and (D). Scale bars: 10 µm in (A–C), 5 µm in (D). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23437151), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

PHD3 depletion stabilizes hypoxic p27 expression by increasing p27 half-life. a Cell cycle arrest at G0 and 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 and 786-O cells. Asterisk indicates significant difference (p < 0,05; n = 3). c Cell cycle arrest at G0 and 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 and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GPR50 phosphorylate and activate T beta RI independently of T beta RII. a SNU638 cells were transfected with the indicated plasmids, stimulated for 1 h with TGF beta (2 ng/mL) and pretreated or not overnight with SB431542 at 10 µM. p-Smad3 and total Smad3 levels and expression of transfected plasmids were determined by western blot in cell lysates. b Co-immunoprecipitation of GRP50 and T beta RI in lysates of SNU638 cells expressing HA-T beta RI alone or together with GPR50 delta 4. Total lysates were used as expression control (c) SNU638 cells were transfected with the indicated plasmids, stimulated TGF beta (2 ng/mL, 1 h). Total T beta RI was immunoprecipitated with anti-Flag antibody and immunoblotted for anti-T beta RIp-S165. Below, the same blot was immunoblotted with anti-Flag to show the amount of T beta RI precipitation in cell lysates. d Phospho-Smad3 and Smad2/3 levels were determined in lysates of SNU638 cells stimulated or not with TGF beta (2 ng/mL, 1 h) and expressing the indicated proteins (as verified by western blot). The myc-MT2 melatonin receptor and the myc-MT2-GPR50Cter served as negative controls. Representative results are shown for all the panels. Similar results were obtained in at least two additional experiments. See also Supplementary Fig. 4 Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41467-018-03609-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Nanog-inducible mouse model.(A) Schematic representation of the K5-rtTA;Col1a1::tetO-Nanog mouse model. The reverse transactivator (rtTA) is under the control of the bovine cytokeratin 5 (K5) promoter. A cassette containing the Nanog-cDNA is under the control of the doxycycline (DOX)-responsive promoter (tetO), which was inserted downstream of the Col1a1 locus. Arrows indicate transcriptional start sites. (B) Relative Nanog mRNA levels in the indicated organs determined by qRT-PCR. Nanog-inducible mice (n = 3) containing both transgenes (K5-rtTAtg/.;Col1a1tetO-Nanog/+; abbreviated as TG) and control mice (n = 3) lacking the transactivator (Col1a1tetO-Nanog/+; abbreviated as CTR) were analyzed 48 hr after administration of doxycycline (DOX) (2 mg/ml) in the drinking water. (C) Immunohistochemistry (IHC) for NANOG of paraffin-embedded sections of tail skin from CTR and TG mice treated as indicated in (B). Two magnifications are shown for each tissue (bars correspond to 50 μm). (D) Nanog mRNA levels normalized to Gapdh in CTR and TG tail skin topically treated 4 times, at 48 hr intervals, with 12-O-tetradecanoylphorbol 13-acetate (TPA) or acetone as a control. Mice (n = 4) were exposed to doxycycline (2 mg/ml) in their drinking water 48 hr prior to TPA treatment and throughout the remaining protocol. (E) Epidermal thickness (basal and suprabasal layers) of CTR and TG mice (n = 5) treated as in (D). (F) Representative hematoxylin and eosin (H&E) staining and immunohistochemistry (IHC) for NANOG, Ki67 and LORICRIN of TPA-treated CTR and TG mice as indicated in (D) (bars correspond to 50 μm). Bars in (B, D, E) correspond to mean ± SD of the indicated number of mice (n). Statistical significance was determined by the two-tailed Student’s t test: (*) p < 0.05; (**) p < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25988972), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

BubR1 associated PP2A, but not KNL1 associated PP1, plays a significant role in the end-on conversion process. a Experimental regime: BubR1 siRNA treated HeLa FRT/TO cells conditionally expressing Venus (YFP)-BubR1 (WT or ∆660–685 mutant) were exposed to Doxycycline for 24 h and MG132 for 1 h prior to immunostaining. b Images of cells treated as in a, immunostained with antibodies against GFP, Tubulin and Astrin and stained with DAPI for DNA. Scale: 5 µm in uncropped and 1 µm in cropped images. Boxed areas correspond to cropped images. c Graph of Astrin intensities on congressed or uncongressed kinetochores in cells expressing Venus (YFP) tagged -BubR1 WT or ∆660–685 mutant, as in b. Horizontal lines show average values (in green) across KTs from two independent experiments. Each circle represents values from one kinetochore. d Images of cells treated as in a, immunostained with antibodies against GFP and Tubulin and CREST anti-sera and stained with DAPI for DNA. Scale: 5 µm in uncropped and 1 µm in cropped images. Boxed areas correspond to cropped images. e Graph shows percentage of lateral vs. end-on kinetochores in Venus-BubR1 (WT or ∆660–685 mutant) expressing cells treated as in d. Each circle represents values from one cell. Black bar marks average values from four independent experiments. f Images of KNL1 siRNA treated HeLa cells expressing LAP-tagged KNL1 WT or mutants (2A or 4A). Following plasmid transfection, cells were exposed to Doxycycline for 1 h and then incubated in Doxycycline-free media for 30 h. Prior to fixation cells were exposed to MG132 for 45 min and immunostained with antibodies against GFP, Tubulin and Astrin. Scale: 5 µm in uncropped and 2 µm in cropped images. Boxed areas correspond to cropped images. g Graph shows percentage of lateral vs. end-on kinetochores in LAP tagged KNL1 (WT, 4A or 2A mutant) expressing cells, treated as in f. Each circle represents values from one cell. Black bar marks average values from three independent experimental repeats. In c, e and g, ‘*’ and # indicate statistically significant and insignificant differences, respectively (assessed using P-values from unpaired Student’s t-test) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28751710), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Regorafenib transcriptionally inhibited VEGF-A expression through decreasing the binding of STAT3 on the promoter of VEGF-A.(A) Top, MDA-MB-231 cells were co-transfected with a Renilla control vector and plasmids containing the firefly luciferase gene driven by wild-type or STAT3 binding site-mutated VEGF-A promoter. After transfection for 48 h, cells were treated with regorafenib for 24 h. Promoter activity was analyzed by luciferase assay after regorafenib treatment. Bottom, MDA-MB-231 cells were transfected with vector-control or STAT3-overexpression plasmid for 48 h. After that, cells were further co-transfected with Renilla and wild-type VEGF-A promoter and detect promoter activity as mentioned above. *p < 0.05, **p < 0.01. (B) After regorafenib treatment for 24 h, STAT3 binding site fragment was detected by PCR in ChIP samples precipitated with STAT3 and rabbit IgG control antibodies in MDA-MB-231 cells. (C,D), MDA-MB-231 cells were transfected, respectively, with control vector or VEGF-A overexpression plasmid (C) or STAT3 overexpression plasmid (D) for 48 h. After transfection, the cells were treated w/wo regorafenib for 24 h and were subjected to western blot assay or seeded to Transwell to analyze the migration ability. *p < 0.05, **p < 0.01. (E) Cells were treated with regorafenib at the indicated dosages for 24 h and then cell lysates were analyzed by SHP-1 phosphatase activity assay. *p < 0.05, **p < 0.01. (F) MDA-MB-231 cells were pretreated with pan-phosphatase inhibitor (left), or specific SHP-1 inhibitor (Middle) for 1 h before regorafenib treatment. Right, MDA-MB-231 cells were transfected, respectively, with control siRNA or SHP-1 siRNA for 48 h. After transfection, the cells were treated w/wo regorafenib (10 μM) for 24 h. The protein levels were analyzed by western blot assay or cells seeded to Transwell to analyze the migration ability. *p < 0.05, **p < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27364975), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, 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
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
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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NB100-56566

TLR4 Antibody (76B357.1) - BSA Free

(5 Reviews)

(138 Publications)

0.1 mg

NB100-56566

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

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

Flow (Intracellular): TLR4 Antibody (76B357.1) [NB100-56566] - Analysis using PE conjugate of NBP2-27149. An intracellular stain was performed on Jurkat cells with TLR4 antibody (76B357.1) NBP2-27149PE (blue) and an isotype control MAB004 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to phycoerythrin.

Immunocytochemistry/Immunofluorescence: TLR4 Antibody (76B357.1) [NB100-56566] - RH-30 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-TLR4 Antibody (76B357.1) NB100-56566 at 1 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunohistochemistry: TLR4 Antibody (76B357.1) [NB100-56566] - Immunofluorescent staining of TMAs. Representative tissue cores from normal (I), adenomatous polyps (II), and CRC (III and IV) are shown. Image collected and cropped by CiteAb from the following publication (//www.jeccr.com/content/33/1/45), licensed under a CC-BY license.

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

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

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - An intracellular stain was performed on RH30 cells with TLR4 Antibody (76B357.1) NB100-56566 (blue) and a matched mouse IgG2b Kappa isotype control (orange) MAB004. Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

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

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

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

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

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

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - An intracellular stain was performed on Jurkat cells with TLR4 Antibody (76B357.1) NB100-56566 (blue) and a matched mouse IgG2b Kappa isotype control (orange) MAB004. Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Flow Cytometry: TLR4 Antibody (76B357.1) [NB100-56566] - An intracellular stain was performed on Raw264.7 cells with TLR4 Antibody (76B357.1) NB100-56566 (blue) and a matched mouse IgG2b Kappa isotype control (orange) MAB004. Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

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

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

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-5031A

Alt Catalog# IMG-5031A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

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

Available Formulations

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

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NB300-605

iNOS Antibody - BSA Free

(3 Reviews)

(121 Publications)

200uL

NB300-605

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

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

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

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

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

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

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

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

Reactivity:

Hu, Mu, Rt, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-605SS

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NBP2-25241

STAT6 Antibody (177C322.1) - BSA Free

(4 Publications)

0.1 mg

NBP2-25241

Reactivity:

Hu, Mu

Species Glossary

Reactivity: Hu, Mu

Applications:

, ,

Applications: , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-6901A

Alt Catalog# IMG-6901A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-25241AF350
Alexa Fluor 405	NBP2-25241AF405
Alexa Fluor 488	NBP2-25241AF488
Alexa Fluor 532	NBP2-25241AF532
Alexa Fluor 594	NBP2-25241AF594
Alexa Fluor 647	NBP2-25241AF647
Alexa Fluor 700	NBP2-25241AF700
Alexa Fluor 750	NBP2-25241AF750
Biotin	NBP2-25241B
DyLight 350	NBP2-25241UV
DyLight 405	NBP2-25241V
DyLight 488	NBP2-25241G
DyLight 550	NBP2-25241R
DyLight 594	NBP2-25241DL594
DyLight 650	NBP2-25241C
DyLight 680	NBP2-25241FR
DyLight 755	NBP2-25241IR
FITC	NBP2-25241F
HRP	NBP2-25241H
Janelia Fluor 549	NBP2-25241JF549
Janelia Fluor 646	NBP2-25241JF646
mFluor Violet 450 SE	NBP2-25241MFV450
mFluor Violet 500 SE	NBP2-25241MFV500
mFluor Violet 610 SE	NBP2-25241MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-25241SS
Azide and BSA Free	NBP2-80965

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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)

HIF-1 alpha Antibody - BSA Free

AIF-1/Iba1 Antibody

HIF-1 alpha Antibody

HIF-1 alpha Antibody (2443B) - BSA Free

HIF-1 alpha Antibody (2443C) - BSA Free

HIF-1 alpha Antibody - BSA Free

NLRP3/NALP3 Antibody - BSA Free

HIF-1 alpha Antibody (H1alpha67)

TLR4 Antibody (76B357.1) - BSA Free

iNOS Antibody - BSA Free

STAT6 Antibody (177C322.1) - BSA Free