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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<0.05 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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(select up to 3 products from this page to compare)

NB100-449

HIF-1 alpha Antibody

(28 Reviews)

(286 Publications)

0.1 ml

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.

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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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NBP2-24729

TLR9 Antibody (26C593.2) - BSA Free

(4 Reviews)

(152 Publications)

0.1 mg

NBP2-24729

<b>Genetic Strategies Validation. </b>Knockdown Validated: TLR9 Antibody (26C593.2) [NBP2-24729] - Expression of TLR-9 protein in HB cells before and after 48 hr of transfection. Beta-actin was used as an internal control. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0092748) licensed under a CC-BY license.

Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Analysis of colonic LP or peritoneal cavity (PerC) of normal mice were evaluated by flow cytometry. B cells were intracellularly stained with the anti-TLR9 antibody after the cell surface staining with anti-B220 and CD5 antibodies, and examined using flow cytometry. N = 3, performed twice. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0146191) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: TLR9 Antibody (26C593.2) [NBP2-24729] - Cbl-b is required for the endocytic transit of TLR9. Representative confocal microscopic images of splenocytes from mice with indicated genotypes. For experiments, cells were stimulated through the BCR (green) for 30 minutes then fixed and stained for TLR9 (blue) and Lamp-1 (red)(n = 3). Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0089792) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: TLR9 Antibody (26C593.2) [NBP2-24729] - Monkey retina tissue. Image from verified customer review.

Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Gating strategy for the detection of TLR-7 and -9 in B cell subsets. PBMC were isolated from whole blood and stained for surface markers before cells were fixed, permeabilised and stained for TLR-9. FSC and SSC were first used to gate out debris and SSC-A and SSC-H was utilized to eliminate duplicates. Further gating was done on CD45 and CD19, to target B cells. To separate between the different B cell populations, we gated on CD27 and IgD (D), followed by TLR-9 expression on these subsets. Data from one representative patient is shown. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0120383) licensed under a CC-BY license.

Western Blot: TLR9 Antibody (26C593.2) [NBP2-24729] - Analysis of TLR9 in A) human PBMC, B) human intestine, C) mouse intestine, and D) rat intestine tissue lysates using this antibody at a dilution of 3 ug/ml.

Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Expression of TLR9 on turbinate epithelial cells from healthy controls compared to turbinate and polyp epithelial cells from patients with CRSwNP, n = 5 (A). Intracellular staining for TLR9 (open histogram, black line) and isotype control (filled histogram) on turbinate epithelial cells from a healthy control (B), turbinate epithelial cells (C) and polyp epithelial cells from a patient (D), analysed using flow cytometry. Results are presented as mean +/- SEM, **P<0.01. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0105618) licensed under a CC-BY license.

TLR9 activation upregulated PD-L1 expression by promoting STAT3 Tyr705 phosphorylation in HCC cells. (A) PD-L1 protein expression after treatment with ODN2216 with different concentrations or the indicated times (different concentrations: 0, 5, 10, or 20uM; times: 0, 6, 12, 24, and 36 hours in 10 uM) in Hep3B cells. PD-L1 protein levels were analyzed by Western blotting. (B) PD-L1 protein expression after treatment with ODN2216 with different concentrations or the indicated times (different concentrations: 0, 2.5, 5, or 10uM; times: 0, 6, 12, 24, and 36 hours in 10 uM) in Huh7 cells. PD-L1 protein levels were analyzed by Western blotting. (C) PD-L1 protein expression after treatment with ODN1585 with different concentrations or the indicated times (different concentrations: 0, 2.5, 5, and 10 uM; times: 0, 6, 12, 24, and 36 hours in 5uM) in Hepa1-6 cells. PD-L1 protein levels were analyzed by Western blotting. (D) PD-L1+ tumor cells were detected by flow cytometry after TLR9 agonist (Hep3B and Huh7 cells with ODN2216; Hepa1-6 cells with ODN1585) treatment with indicated concentration. (values are mean +/- SD, *p < 0.05, **p < 0.01, ***p<0.001, NS indicates no significance). (E) PD-L1 expression after TLR9 overexpression in Huh7 cells. PD-L1 expression levels were analyzed by immunofluorescence. (F) PD-L1 protein expression after TLR9 overexpression in Huh7 cells. PD-L1 protein levels were analyzed by Western blotting. (G) PD-L1 protein expression in TLR9 knockdown or TLR9 rescue Hep3B cells. PD-L1 protein levels were analyzed by Western blotting. (H and I) mRNA levels of PD-L1 in Hep3B (H) and Huh7 (I) cells measured by qRT-PCR after stimulation with different concentrations of ODN2216. (values are mean +/- SD, *p < 0.05, **p < 0.01, NS indicates no significance) (J) TLR9 overexpression-induced PD-L1 expression after MYC, JUN, IRF1, IRF3, STAT1 or STAT3 silencing. PD-L1 mRNA expression in Huh7 cells was analyzed after TLR9 overexpression alone or in the presence of MYC-, JUN-, IRF1-, IRF3-, STAT1- or STAT3-specific siRNA or siRNA-NC. (values are mean +/- SD, ***p<0.001). (K) p-STAT3 (Tyr705) levels in Hep3B cells after treatment with different concentrations of ODN2216 (a TLR9 agonist; ODN2216: 0, 2.5, 5, or 10uM) analyzed by Western blotting. (L) p-STAT3 (Tyr705) levels after TLR9 overexpression in Huh7 cells analyzed by Western blotting. (M) TLR9 overexpression-induced p-STAT3 (Tyr705) levels after TLR9 inhibition. p-STAT3 (Tyr705) levels were analyzed after TLR9 overexpression alone or in the presence of the TLR9 antagonist chloroquine diphosphate. (N) p-STAT3-induced PD-L1 levels after STAT3 inhibition. PD-L1 levels were analyzed after TLR9 overexpression alone or in the presence of the STAT3-specific small molecular inhibitor BP-1-102. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32483468), licensed under a CC-BY licence.

THP-1 human acute monocytic leukemia cell line was stained with Mouse anti-TLR9 (26C593.2) Protein-G purified Monoclonal Antibody conjugated to Janelia Fluor® 549 (Catalog # NBP2-24729JF549, blue histogram) or matched control antibody (orange histogram).

Reactivity:

Hu, Mu, Rt, Ca, Eq, Pm, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Eq, Pm, Pm

Applications:

, , , , , , , , , , ,

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

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-305A

Alt Catalog# IMG-305A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-24729AF350
Alexa Fluor 405	NBP2-24729AF405
Alexa Fluor 488	NBP2-24729AF488
Alexa Fluor 532	NBP2-24729AF532
Alexa Fluor 594	NBP2-24729AF594
Alexa Fluor 647	NBP2-24729AF647
Alexa Fluor 700	NBP2-24729AF700
Alexa Fluor 750	NBP2-24729AF750
Allophycocyanin	NBP2-24729APC
Biotin	NBP2-24729B
Biotin	NBP2-24890
DyLight 350	NBP2-24729UV
DyLight 405	NBP2-24729V
DyLight 488	NBP2-24729G
DyLight 550	NBP2-24729R
DyLight 594	NBP2-24729DL594
DyLight 650	NBP2-24729C
DyLight 680	NBP2-24729FR
DyLight 755	NBP2-24729IR
FITC	NBP2-24729F
HRP	NBP2-24729H
Janelia Fluor 549	NBP2-24729JF549
Janelia Fluor 646	NBP2-24729JF646
PE	NBP2-24907
PE	NBP2-24729PE
PerCP	NBP2-24729PCP
mFluor Violet 450 SE	NBP2-24729MFV450
mFluor Violet 500 SE	NBP2-24729MFV500
mFluor Violet 610 SE	NBP2-24729MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Azide Free	NBP2-24863
BSA Free	NBP2-24729SS

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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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NBP2-24875

TLR3 Antibody (40C1285.6) - BSA Free

(87 Publications)

0.1 mg

NBP2-24875

Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Mouse colon using TLR3 antibody (clone 40C1285.6) at 1:500 dilution with HRP-DAB detection and hematoxylin counterstaining. Intense signal was found in subset of cells at the bases of the crypts.

Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 in Fravel, L363, OPM1, RPMI8226, XG1, and NCI-H929 as determined by flow cytometry. HCMLs were stained using an intracellular staining protocol with TLR3 antibodies followed by relevant secondary fluorescent-conjugated antibodies. Filled histograms (purple) represent the isotype controls and the open histograms (red) indicate TLR3. Data are representative for analysis of >=2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license.

Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - Analysis of TLR3 in lysates from A) human intestine and F) ovary using TLR3 antibody at 3 ug/ml. Goat anti-mouse HRP conjugate was used as secondary.

Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - HEK293T cells were transfected with TLR3, TLR3-9-3 and TLR3-3-9. Western blot was performed using anti-TLR3 or anti-HA antibodies. Anti-Beta-actin antibodies were used as a loading control. The representative data from three experiments are shown. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0092391) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Tissue section of mouse intestine using TLR3 antibody (clone 40C1285.6) at 1:500 dilution with HRP-DAB detection and hematoxylin counterstaining. The representative image shows a punctate staining of the ER and endosomes in a subset of cells in Peyer's patches (organized lymphoid nodules) in the tested section.

Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Analysis of TLR3 in (A) human gut lumen (longitudinal section, transverse region) using this antibody at 10 ug/ml (Data courtesy Dr. Elizabeth Furrie, University of Dundee) and mouse spleen tissue using isotype control (B) and this antibody (C) at 5 mg/ml.

NDRG2 inhibits cell proliferation and reduces the intracellular glucose levels of breast cancer cells. (A) T-47D, MCF-7, Bcap37, MDA-MB-231 and SK-BR-3 cells were collected for the extraction of proteins and analysed for N-myc downstream-regulated gene 2 (NDRG2) expression by immunoblotting. (B) SK-BR-3 cells with low NDRG2 expression were infected by an adenovirus carrying NDRG2 (Ad-NDRG2) or negative control LacZ (Ad-LacZ), and T-47D cells with high NDRG2 were transfected with small interfering RNA targeting NDRG2 (NDRG2 siRNA) or negative control siRNA (Con siRNA). Thereafter proteins were extracted from these cells and analysed by immunoblotting. beta -actin was used as a loading control. Before being cultured in 25 mM high-glucose (H.G.) or 5.5 mM low-glucose (L.G.) medium, SK-BR-3 cells were infected by Ad-NDRG2 (C) and T-47D cells were transfected by NDRG2 siRNA (D). Cell proliferation was detected by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay for 1 to 5 days. (C) and (D) The data presented are means ± SD for three independent experiments; error bars represent SD from 8 replicative wells. (C) *P < 0.05 and **P < 0.01 versus H.G. Ad-LacZ. #P < 0.05 versus L.G. Ad-LacZ. (D) *P < 0.05 versus H.G. Con siRNA. (E) and (F) SK-BR-3 cells were cultured to glucose medium at concentrations of 0, 5, 25, 50 and 100 mM for 24 hours, and then the protein or mRNA was extracted for analysis by immunoblotting (E) or real-time PCR (F). beta -actin was used as a loading control. The data presented are means ± SD; error bars represented SD from 3 replicative wells. *P < 0.05 and **P < 0.01 versus control group. (G) SK-BR-3 or (H) T-47D cells, respectively, were infected with Ad-NDRG2 or transfected NDRG2 siRNA and cultured in a high-glucose medium (25 mM) for 48 hours. Next, cell glucose concentrations were measured. (G) and (H) The data presented are means ± SD of three independent experiments; error bars represent SD from 8 replicative wells. *P < 0.05 and **P < 0.01 versus control group. Image collected and cropped by CiteAb from the following open publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3628), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Characterization of selected mutant protein glycosylation status or localization.(A) Two independent, representative experiments to analyze the glycosylation status of GFP-NPC1 wild type and GFP-NPC1 P251C/L929C, as determined by immunoblot of indicated samples with anti-GFP antibodies after 6% SDS PAGE; samples were incubated at 70°C in SDS PAGE sample buffer for 10 min prior to loading. Molecular weight markers are shown at left in kilodaltons here and in all subsequent gels shown. (B), Localization of NPC1 P251/L929C/P249K/P259K in NPC1−/− HeLa cells as in Figure 1C. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32410728), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Notch-1 is identified as an intermediate molecule in the miR-1956-VEGF axis. (A) Notch-1 is a target gene for miR-1956. The sequence of miR-1956, the potential binding site at the 3' UTR of Notch-1 mRNA, and the nucleotides mutated in the Notch-1-3' UTR mutant are shown. HEK293 cells were transiently cotransfected with miR-1956 mimic or NC using luciferase reporter vectors. The luciferase activity was normalized to the activity of Renilla luciferase. Data are shown as mean ± SD from three independent experiments. *, significantly different from NC; **, p < 0.01. After transfection with 50 nmol/L of miR-1956 mimic for 3 days, the mRNA level of Notch-1 was determined using qRT-PCR (B), and the protein expression of Notch-1 was measured using western blotting (C). For B, data are shown as mean ± SD from three independent experiments. *, significantly different from control; **, p < 0.01. For C, representative images of two independent experiments are shown. Data are shown as mean ± SD. *, significantly different from control; **, p < 0.01. ADMSCs were transfected with 2.5 μg Notch-1 plasmid and 50 nmol/L miR-1956 mimic or 100 nmol/L miR-1956 inhibitor for 3 days, the intracellular expression of Notch-1 (D) and VEGF (E) was detected by western blotting. For D and E, representative images of four independent experiments are shown. Data are shown as mean ± SD. *, significantly different from the control group transfected with control plasmid and NC mimic or inhibitor; *, p < 0.01; **, p < 0.01. #, significantly different from the group transfected with Notch-1 plasmid and NC mimic or inhibitor; #, p < 0.05. One-way ANOVA followed by Tukey's post-test was performed (A-E). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31938051), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ca

Species Glossary

Reactivity: Hu, Mu, Ca

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-315A

Alt Catalog# IMG-315A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-24875AF350
Alexa Fluor 405	NBP2-24875AF405
Alexa Fluor 488	NBP2-24875AF488
Alexa Fluor 532	NBP2-24875AF532
Alexa Fluor 594	NBP2-24875AF594
Alexa Fluor 647	NBP2-24875AF647
Alexa Fluor 700	NBP2-24875AF700
Alexa Fluor 750	NBP2-24875AF750
Allophycocyanin	NBP2-24875APC
Biotin	NBP2-24875B
Biotin	NBP2-24782
DyLight 350	NBP2-24875UV
DyLight 405	NBP2-24875V
DyLight 488	NBP2-24875G
DyLight 550	NBP2-24875R
DyLight 594	NBP2-24875DL594
DyLight 650	NBP2-24875C
DyLight 680	NBP2-24875FR
DyLight 755	NBP2-24875IR
FITC	NBP2-24875F
HRP	NBP2-24875H
Janelia Fluor 549	NBP2-24875JF549
Janelia Fluor 646	NBP2-24875JF646
PE	NBP2-24902
PE	NBP2-24875PE
PerCP	NBP2-24875PCP
mFluor Violet 450 SE	NBP2-24875MFV450
mFluor Violet 500 SE	NBP2-24875MFV500
mFluor Violet 610 SE	NBP2-24875MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-24875SS
Azide Free	NBP2-33263

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NBP2-24906

TLR7 Antibody - BSA Free

(4 Reviews)

(78 Publications)

0.1 mg

NBP2-24906

Immunocytochemistry/Immunofluorescence: TLR7 Antibody [NBP2-24906] - Immunolocalization of TLR7 (A) and glial fibrillary acidic protein (GFAP) (B) in murine myenteric plexus. Most of the GFAP positive cells were also positive for TLR7 in the merged image (C, yellow staining). (Courtesy of Barajon I, et al., Journal of Histochemistry and Cytochemistry, 57(11): 1013-;1023, 2009.)

Immunohistochemistry: TLR7 Antibody [NBP2-24906] - Expression of the TLRs 5 and 7 were evaluated in the PDAC tissue by their staining intensity using TLR5 antibody (NBP2-24787) and TLR7 antibody (NBP2-24906). Note negative staining in E and G; positive staining in F and H. For TLR7 immunopositivity was detectable in the cytoplasm with no notable membranous or nuclear positivity. TLR5 showed distinctive nuclear positivity, and detectable positivity in the cytoplasm in some samples. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0219245) licensed under a CC-BY license.

Immunohistochemistry-Frozen: TLR7 Antibody [NBP2-24906] - analysis of frozen mouse ear skin tissue using anti-TLR7 antibody. Image from verified customer review.

Immunohistochemistry-Frozen: TLR7 Antibody [NBP2-24906] - analysis of TLR7 in acetone-fixed, frozen mouse ear skin section using anti-TLR7 antibody. Image from verified customer review.

Western Blot: TLR7 Antibody [NBP2-24906] - Analysis using the Azide Free version of NBP2-24906. Detection of TLR7 in RAW cell lysate using this antibody.

Immunocytochemistry/Immunofluorescence: TLR7 Antibody [NBP2-24906] - Analysis using the Azide Free version of NBP2-24906. Staining of Raw 246.7 cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). Image objective 40x. An antibody dilution of 1:10 was used.

Immunohistochemistry-Paraffin: TLR7 Antibody - BSA Free [NBP2-24906] - Analysis of a FFPE tissue section of human skin using 1:200 dilution of TLR7 antibody (NBP2-24906). The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.

Expression of TLR7 in lung tissues of non-smokers, smokers, and COPD patients. Total protein and mRNA were obtained from lung tissues of non-smokers (n = 15), smokers (n = 12), and COPD patients (n = 15). (E) Representative immunohistochemistry images are shown. The control IgG isotype showed negative staining. Data are presented as individual values and mean +/- standard deviation. Exact P values were obtained using Kruskal-Wallis and Dunn's post-hoc tests. Image collected and cropped by CiteAb from the following publication (//respiratory-research.biomedcentral.com/articles/10.1186/s12931-015-0179-5), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-581A

Alt Catalog# IMG-581A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-24906AF350
Alexa Fluor 405	NBP2-24906AF405
Alexa Fluor 488	NBP2-24906AF488
Alexa Fluor 532	NBP2-24906AF532
Alexa Fluor 594	NBP2-24906AF594
Alexa Fluor 647	NBP2-24906AF647
Alexa Fluor 700	NBP2-24906AF700
Alexa Fluor 750	NBP2-24906AF750
Allophycocyanin	NBP2-24906APC
Biotin	NBP2-24906B
DyLight 350	NBP2-24906UV
DyLight 405	NBP2-24906V
DyLight 488	NBP2-24906G
DyLight 550	NBP2-24906R
DyLight 594	NBP2-24906DL594
DyLight 650	NBP2-24906C
DyLight 680	NBP2-24906FR
DyLight 755	NBP2-24906IR
FITC	NBP2-24777
HRP	NBP2-24906H
Janelia Fluor 549	NBP2-24906JF549
Janelia Fluor 646	NBP2-24906JF646
PE	NBP2-24906PE
PE	NBP2-31071
PerCP	NBP2-24906PCP
mFluor Violet 450 SE	NBP2-24906MFV450
mFluor Violet 500 SE	NBP2-24906MFV500
mFluor Violet 610 SE	NBP2-24906MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Azide Free	NBP2-24905
Azide Free	NBP2-24905SS
BSA Free	NBP2-24906SS

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NB100-683

CD68/SR-D1 Antibody (KP1) - BSA Free

(1 Review)

(66 Publications)

0.1 mg

NB100-683

Immunocytochemistry/Immunofluorescence: CD68/SR-D1 Antibody (KP1) [NB100-683] - A431 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 CD68/SR-D1 Antibody [KP1] (NB100-683) 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.

Western Blot: CD68/SR-D1 Antibody (KP1) [NB100-683] - Total protein from mouse Raw cells was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/ml anti-CD68 (NB100-683) in blocking buffer and detected with an anti-mouse HRP secondary antibody using NovaLume chemiluminescence detection reagent (NPB2-61915).

Flow Cytometry: CD68/SR-D1 Antibody (KP1) [NB100-683] - An intracellular stain was performed on A431 cells with CD68/SR-D1 [KP1] Antibody NB100-683AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Immunohistochemistry-Paraffin: CD68/SR-D1 Antibody (KP1) [NB100-683] - Analysis of a FFPE tissue section of human spleen using 1:200 dilution of CD68 antibody. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.

Flow Cytometry: CD68/SR-D1 Antibody (KP1) [NB100-683] - An intracellular stain was performed on THP-1 cells with CD68 Antibody [KP1] NB100-683 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Dual RNAscope ISH-IHC: CD68/SR-D1 Antibody (KP1) [NB100-683] - NOS2 mRNA (red) and CD68 protein (green) were detected in formalin-fixed paraffin-embedded tissue sections of human breast cancer. ACD's Integrated Co-Detection Workflow was performed using ACD RNAScope Probe Hs-NOS2 and CD68/SR-D1 antibody (KP1) at 1:100 dilution. Tissue was stained on Leica Bond RX using RNAscope (TM) 2.5 LS Reagent Kit-RED, BOND Polymer Refine Detection (DAB) and Hematoxylin, BOND Polymer Refine Red Detection and Hematoxylin and RNAscope (TM) 2.5 LS Green Accessory Pack. Tissue was counterstained with 50% hematoxylin (blue).

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-683AF350
Alexa Fluor 405	NB100-683AF405
Alexa Fluor 488	NB100-683AF488
Alexa Fluor 532	NB100-683AF532
Alexa Fluor 594	NB100-683AF594
Alexa Fluor 647	NB100-683AF647
Alexa Fluor 700	NB100-683AF700
Alexa Fluor 750	NB100-683AF750
Allophycocyanin	NB100-683APC
Biotin	NB100-683B
DyLight 350	NB100-683UV
DyLight 405	NB100-683V
DyLight 488	NB100-683G
DyLight 550	NB100-683R
DyLight 594	NB100-683DL594
DyLight 650	NB100-683C
DyLight 680	NB100-683FR
DyLight 755	NB100-683IR
FITC	NB100-683F
HRP	NB100-683H
Janelia Fluor 549	NB100-683JF549
Janelia Fluor 646	NB100-683JF646
PE	NB100-683PE
PerCP	NB100-683PCP
mFluor Violet 450 SE	NB100-683MFV450
mFluor Violet 500 SE	NB100-683MFV500
mFluor Violet 610 SE	NB100-683MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-683-0.025mg

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NBP2-42225

CD63 Antibody (H5C6) - BSA Free

(5 Reviews)

(53 Publications)

0.1 ml

NBP2-42225

Immunocytochemistry/Immunofluorescence: CD63 Antibody (H5C6) [NBP2-42225] - HeLa 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-CD63 Antibody [H5C6] conjugated to DyLight 550 (NBP2-42225R) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - An intracellular stain was performed on SK-MEL-28 cells with CD63 (H5C6) Antibody NBP2-42225R (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.

Immunocytochemistry/Immunofluorescence: CD63 Antibody (H5C6) [NBP2-42225] - MDCK cells stained with CD63 antibody at a dilution of 1:50 followed by Donkey anti-mouse secondary antibody conjugated with Alexa Fluor 488 (1:500). Nuclei were stained with Hoechst 33342. ICC/IF image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: CD63 Antibody (H5C6) [NBP2-42225] - U2OS 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-CD63 Antibody [H5C6] conjugated to Alexa Fluor 488 (NBP2-42225AF488) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: CD63 Antibody (H5C6) [NBP2-42225] - A431 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-CD63 Antibody [H5C6] conjugated to Biotin (NBP2-42225B) at 5 ug/ml for 60 minutes at room temperature and detected with Streptavidin Protein conjugated to DyLight 488 at a 1:500 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: CD63 Antibody (H5C6) [NBP2-42225] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-CD63 [H5C6] conjugated to Alexa Fluor 488 [NBP2-42225AF488] at 10ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Western Blot: CD63 Antibody (H5C6) - BSA Free [NBP2-42225] - Analysis of common EV markers, where 10 ug of total protein was loaded in each lane. cASCs-EVs expressed CD63 and CD9, while beta actin and lamin A showed lower expression. The displayed data represent at least three repeated experiments with consistent results. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32040478/) licensed under a CC-BY license.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - An intracellular stain was performed on HeLa cells with CD63 [H5C6] Antibody NBP2-42225AF594 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 594.

Western Blot: CD63 Antibody (H5C6) [NBP2-42225] - The same samples and volumes were run under reducing and non-reducing conditions. All procedures were performed in parallel for both conditions. L- ladder +- exosomes. Image visualized with HRP linked to secondary antibody. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: CD63 Antibody (H5C6) [NBP2-42225] - HEK cells stained with CD63 antibody at a dilution of 1:50 followed by Donkey anti-mouse secondary antibody conjugated with Alexa Fluor 488 (1:500). Nuclei were stained with Hoechst 33342. ICC/IF image submitted by a verified customer review.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - Human peripheral blood cells were stained (2 x 10^6 cells/mL) using the anti-CD63 antibody (Blue) at a dilution of 1:1000. Signal was detected using a Gt x Ms DyLight 488 Secondary and gated to the monocyte/granulocyte cell populations. Isotype was Mouse IgG1 kappa (orange). Data collected on BD FACS Calibur flow cytometer.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - A431 cells were stained (1 x10^6 cells/mL) using the anti-CD63 antibody at a 1:1000 dilution (blue). Signal was detected with Gt x Ms DyLight 488 secondary. Isotype control (orange).

Flow (Intracellular): CD63 Antibody (H5C6) [NBP2-42225] - An intracellular stain was performed on HepG2 cells with CD63 Antibody (H5C6) NBP2-42225AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - An intracellular stain was performed on HeLa cells with CD63 Antibody (H5C6) NBP2-42225APC (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Allophycocyanin.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - An intracellular stain was performed on SK-MEL-28 cells with CD63 Antibody (H5C6) NBP2-42225AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Flow Cytometry: CD63 Antibody (H5C6) [NBP2-42225] - An intracellular stain was performed on HeLa cells with CD63 [H5C6] Antibody NBP2-42225AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

NCAM as a neuronal exosome marker in plasma. (H) Western blot analysis of NCAM and CD63 from EVs released from iPSCs, iPSC-derived cortical neurons, and iPSC-derived brain organoids. EVs were isolated using SEC from the cell culture media of each sample, and equal EV particle numbers (6 x 108) were subject to immunoblotting with NCAM and CD63 antibodies. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35655952), licensed under a CC-BY licence.

Characterization of cASC-EVs. (D) Immunoblotting analysis of common EV markers, where 10 ug of total protein was loaded in each lane. cASCs-EVs expressed CD63 and CD9, while beta actin and lamin A showed lower expression. The displayed data represent at least three repeated experiments with consistent results. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32040478), licensed under a CC-BY licence.

CD63 (H5C6) was detected in immersion fixed MCF7 human breast cancer cell line using Mouse anti-CD63 (H5C6) Protein G Purified Monoclonal Antibody conjugated to Alexa Fluor® 488 (Catalog # NBP2-42225AF488) (green) at 5 µg/mL overnight at 4C. Cells were counterstained with DAPI (blue). Cells were imaged using a 100X objective and digitally deconvolved.

CD63 (H5C6) was detected in immersion fixed A431 human skin carcinoma cell line using Mouse anti-CD63 (H5C6) Protein-G purified Monoclonal Antibody conjugated to DyLight 550 (Catalog # NBP2-42225R) (red) at 5 µg/mL overnight at 4C. Cells were counterstained with DAPI (blue). Cells were imaged using a 100X objective and digitally deconvolved.

Reactivity:

Hu, Ca

Species Glossary

Reactivity: Hu, Ca

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-42225AF350
Alexa Fluor 405	NBP2-42225AF405
Alexa Fluor 488	NBP2-42225AF488
Alexa Fluor 532	NBP2-42225AF532
Alexa Fluor 594	NBP2-42225AF594
Alexa Fluor 647	NBP2-42225AF647
Alexa Fluor 700	NBP2-42225AF700
Alexa Fluor 750	NBP2-42225AF750
Allophycocyanin	NBP2-42225APC
Allophycocyanin/Cy7	NBP2-42225APCCY7
Biotin	NBP2-42225B
DyLight 350	NBP2-42225UV
DyLight 405	NBP2-42225V
DyLight 488	NBP2-42225G
DyLight 550	NBP2-42225R
DyLight 594	NBP2-42225DL594
DyLight 650	NBP2-42225C
DyLight 680	NBP2-42225FR
DyLight 755	NBP2-42225IR
FITC	NBP2-42225F
HRP	NBP2-42225H
Janelia Fluor 549	NBP2-42225JF549
Janelia Fluor 646	NBP2-42225JF646
PE	NBP2-42225PE
PE/Atto594	NBP2-42225PEATT594
PE/Cy5.5	NBP2-42225PECY55
PE/Cy7	NBP2-42225PECY7
PerCP	NBP2-42225PCP
mFluor Violet 450 SE	NBP2-42225MFV450
mFluor Violet 500 SE	NBP2-42225MFV500
mFluor Violet 610 SE	NBP2-42225MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-42225SS
Azide and BSA Free	NBP2-80654

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NB600-235

BLIMP1/PRDM1 Antibody (3H2-E8) - BSA Free

(2 Reviews)

(52 Publications)

0.1 ml

NB600-235

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) - BSA Free [NB600-235] - An intracellular stain was performed on A431 cells with BLIMP1/PRDM1 Antibody (3H2-E8) NB600-235 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).

Western Blot: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - Detection of Blimp-1 in murine plasmacytoma cell lysate (P3X) using NB 600-235. 1881: murine pre-B cell lysate (negative control). Photo courtesy of DA Savitsky, Columbia University.

Immunocytochemistry/Immunofluorescence: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - Double IF for Blimp-1 (green) and Ki-67 (proliferation, red) with DAPI counterstain, at 10x magnification (scale bar is 10um). Positive surface epithelium and centrocytes are labelled. Photo courtesy of Dr. Giorgio Cattoretti, Institute for Cancer Genetics, Columbia University, NY.

Immunocytochemistry/Immunofluorescence: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-BLIMP1/PRDM1 (3H2-E8) conjugated to DyLight 550 [NB600-235R] at 20ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - IL-10+Blimp-1-, IL-10+Blimp-1+, IL-10-Blimp-1+ and IL-10-Blimp-1- cells, % total living single splenic CD19+ cells of 3 total mice (Tedder Lab; Duke Univ).

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - Blimp-1 expression by IL-10+ (black line), IL-10- (dotted line) or CD8+ (thin, shaded line) cells (Tedder Lab; Duke Univ)

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - Blimp-1 expression by CD19+ (thick black line) or CD8+ (thin, shaded line). (Tedder Lab; Duke Univ).

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - Analysis using the Biotin conjugate of NB600-235. Staining of Blimp-1 in mouse spleen. Image courtesy of product review by Branislav Krljanac.

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - An intracellular stain was performed on U266 cells with BLIMP1/PRDM1 Antibody (3H2-E8) NB600-235 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and 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 F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems).

Flow Cytometry: BLIMP1/PRDM1 Antibody (3H2-E8) [NB600-235] - An intracellular stain was performed on A431 cells with BLIMP1/PRDM1 [3H2-E8] Antibody NB600-235C (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 650.

DenA deneddylase activity.(A) Recombinant human DEN1 and fungal DenA deneddylate a human CUL1-Nedd8 substrate in vitro. SDS-PAGE and subsequent western analysis show cleavage of the substrate (∼60 kDa) producing the C-terminal CUL1 (∼50 kDa) as outlined in experimental procedures. (B) Deneddylation test in a heterologous yeast system. A. nidulans DenA can remove Rub1 from CulD in heterologous expression experiments in S. cerevisiae. DenA was expressed as native protein or C-terminally fused with a V5/His6 epitope tag. Both variants were driven by the inducible GAL1 promoter. CulD, N-terminal-fused with the LexA activation domain, was expressed under control of the constitutive ADH promoter. A. nidulans proteins were expressed in S. cerevisiae wild type and delta csn5 background. Western analysis with antibodies against Rub1 ( alpha -Rub1), the LexA epitope ( alpha -LexA) and the V5 epitope ( alpha -V5) were performed. Detection with alpha -Rub1 generated two additional signals upon culD expression, representing LexA-CulD and a second CulD pool where LexA was unspecifically cleaved off. Both signals disappeared upon co-expression of DenA indicating deneddylation activity (red arrows). The slower migrating signal of alpha -LexA western experiments corresponded to Rub1 modified LexA-CulD. This signal was absent when DenA was co-expressed. Detection of the V5 tag was applied to monitor DenA expression. The neddylated yeast cullin migrating at around 100 kDa was not affected by DenA activity. (C) Deneddylation of fungal CulA by CSN and DenA. Whole cell lysates of A. nidulans wild type, delta csnE and delta denA were probed with alpha -CulA. The ratio of neddylated CulA (CulA*N8; ∼106 kDa*) to non-neddylated CulA (∼96 kDa**) was calculated from three independent experiments. Membranes were reprobed with alpha -Actin ( alpha -ACT) for normalization. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pgen.1003275), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Histone induce BMECs pyroptosis is dependent on activations of caspase 1, caspase 3 and NLRP3. BMECs were incubated with stimulated histone for 16 h, and the activities of these proteins were determined by western blotting. Date are presented as mean ± SEM (n = 5). P-values of < 0.05 were considered significant (**P < 0.01, ***P < 0.001, and “ns” means not significant). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31156617), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Po

Species Glossary

Reactivity: Hu, Mu, Po

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	NB600-235AF350
Alexa Fluor 405	NB600-235AF405
Alexa Fluor 488	NB600-235AF488
Alexa Fluor 532	NB600-235AF532
Alexa Fluor 594	NB600-235AF594
Alexa Fluor 647	NB600-235AF647
Alexa Fluor 700	NB600-235AF700
Alexa Fluor 750	NB600-235AF750
Allophycocyanin	NB600-235APC
Biotin	NB600-235B
DyLight 350	NB600-235UV
DyLight 405	NB600-235V
DyLight 488	NB600-235G
DyLight 550	NB600-235R
DyLight 594	NB600-235DL594
DyLight 650	NB600-235C
DyLight 680	NB600-235FR
DyLight 755	NB600-235IR
FITC	NB600-235F
HRP	NB600-235H
Janelia Fluor 549	NB600-235JF549
Janelia Fluor 646	NB600-235JF646
PE	NB600-235PE
PerCP	NB600-235PCP
mFluor Violet 450 SE	NB600-235MFV450
mFluor Violet 500 SE	NB600-235MFV500
mFluor Violet 610 SE	NB600-235MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB600-235SS
Azide and BSA Free	NBP2-80597

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NBP1-19371

CD4 Antibody - BSA Free

(9 Reviews)

(49 Publications)

0.1 ml

NBP1-19371

Western Blot: CD4 Antibody [NBP1-19371] - CD4 antibody was tested in the following cell lysates: 1) human spleen 2) human tonsil 3) human placenta 4) human kidney 5) human liver 6) mouse spleen 7) mouse placenta 8) rat placenta.

Immunocytochemistry/Immunofluorescence: CD4 Antibody [NBP1-19371] - CD4 antibody was tested in Jurkat cells with DyLight 488 (green). Nuclei were counterstained with DAPI (blue).

Flow Cytometry: CD4 Antibody - BSA Free [NBP1-19371] - An intracellular stain was performed on U-251 MG cells with CD4 Antibody NBP1-19371AF594 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 594.

Western Blot: CD4 Antibody [NBP1-19371] - Mouse spleen, 25ug total protein. Image from verified customer review.

Immunohistochemistry-Paraffin: CD4 Antibody [NBP1-19371] - Staining of paraffin-embedded mouse brain tissue. Photo courtesy of product review by verified customer.

Immunohistochemistry-Paraffin: CD4 Antibody [NBP1-19371] - Analysis of a FFPE tissue section of mouse brain using CD4 antibody at 1:300 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody primarily generated a strong signal in the membranes of a subset of cells in the tested section.

Immunohistochemistry-Paraffin: CD4 Antibody [NBP1-19371] - Analysis of a FFPE section of mouse spleen using CD4 antibody at 1:300 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody generated a strong signal in the membranes of a subset of cells in the spleen section and the staining showed punctate appearance in some cells.

Immunohistochemistry-Frozen: CD4 Antibody [NBP1-19371] - Staining in mouse liver tissue.

Immunohistochemistry-Paraffin: CD4 Antibody [NBP1-19371] - Alcohol-fixed paraffin-embedded rat spleen tissue. Dilution 1:150. Image from verified customer review.

Flow Cytometry: CD4 Antibody [NBP1-19371] - An intracellular stain was performed on Jurkat cells with CD4 Antibody NBP1-19371R (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.

Flow Cytometry: CD4 Antibody [NBP1-19371] - An intracellular stain was performed on Jurkat cells with CD4 Antibody NBP1-19371AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Flow Cytometry: CD4 Antibody [NBP1-19371] - An intracellular stain was performed on U937 cells with CD4 Antibody NBP1-19371AF594 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 594.

Flow Cytometry: CD4 Antibody [NBP1-19371] - An intracellular stain was performed on U937 cells with CD4 Antibody NBP1-19371G (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 488.

Simple Western: CD4 Antibody [NBP1-19371] - Lane view shows a specific band for CD4 in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Dual RNAscope ISH-IHC: CD4 Antibody [NBP1-19371] - IFNG mRNA (red) and CD4 protein (green) were detected in formalin-fixed paraffin-embedded tissue sections of human lung cancer. ACD's Integrated Co-Detection Workflow was performed using ACD RNAScope Probe Hs-IFNG and CD4 antibody at 1:100 dilution. Tissue was stained on Leica Bond RX using RNAscope (TM) 2.5 LS Reagent Kit-RED, BOND Polymer Refine Detection (DAB) and Hematoxylin (Cat. No. DS9800), BOND Polymer Refine Red Detection and Hematoxylin and RNAscope (TM) 2.5 LS Green Accessory Pack. Tissue was counterstained with 50% hematoxylin (blue).

Dual RNAscope ISH-IHC: CD4 Antibody [NBP1-19371] - CCR5 mRNA (red) and CD4 protein (green) were detected in formalin-fixed paraffin-embedded tissue sections of human lung cancer. ACD's Integrated Co-Detection Workflow was performed using ACD RNAScope Probe Hs-CCR5 and CD4 antibody at 1:100 dilution. Tissue was stained on Leica Bond RX using RNAscope (TM) 2.5 LS Reagent Kit-RED, BOND Polymer Refine Detection (DAB) and Hematoxylin, BOND Polymer Refine Red Detection and Hematoxylin and RNAscope (TM) 2.5 LS Green Accessory Pack. Tissue was counterstained with 50% hematoxylin (blue).

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

Reactivity:

Hu, Mu, Rt, Po, Ca, Rb

Species Glossary

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

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-19371AF350
Alexa Fluor 405	NBP1-19371AF405
Alexa Fluor 488	NBP1-19371AF488
Alexa Fluor 532	NBP1-19371AF532
Alexa Fluor 594	NBP1-19371AF594
Alexa Fluor 647	NBP1-19371AF647
Alexa Fluor 700	NBP1-19371AF700
Alexa Fluor 750	NBP1-19371AF750
Allophycocyanin	NBP1-19371APC
Biotin	NBP1-19371B
DyLight 350	NBP1-19371UV
DyLight 405	NBP1-19371V
DyLight 488	NBP1-19371G
DyLight 550	NBP1-19371R
DyLight 594	NBP1-19371DL594
DyLight 650	NBP1-19371C
DyLight 680	NBP1-19371FR
DyLight 755	NBP1-19371IR
FITC	NBP1-19371F
HRP	NBP1-19371H
Janelia Fluor 549	NBP1-19371JF549
Janelia Fluor 646	NBP1-19371JF646
PerCP	NBP1-19371PCP
mFluor Violet 450 SE	NBP1-19371MFV450
mFluor Violet 500 SE	NBP1-19371MFV500
mFluor Violet 610 SE	NBP1-19371MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-19371SS

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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

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Clone

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Species Glossary

HIF-1 alpha Antibody (H1alpha67)

HIF-1 alpha Antibody - BSA Free

HIF-1 alpha Antibody

NLRP3/NALP3 Antibody - BSA Free

TLR9 Antibody (26C593.2) - BSA Free

TLR4 Antibody (76B357.1) - BSA Free

TLR3 Antibody (40C1285.6) - BSA Free

TLR7 Antibody - BSA Free

CD68/SR-D1 Antibody (KP1) - BSA Free

CD63 Antibody (H5C6) - BSA Free

BLIMP1/PRDM1 Antibody (3H2-E8) - BSA Free

CD4 Antibody - BSA Free