| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-135SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56519SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56506SS | |||
| Azide and BSA Free | NBP2-33212 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-58358SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-131SS | |||
| Azide and BSA Free | NBP2-80762 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2288SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-582SS | |||
| Azide and BSA Free | NBP2-80959 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-39002SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2215SS | |||
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Mouse liver tissue lysate, 10 ug total protein per lane, probed with CHREBP antibody. Specific bands at ~150 kDa (some wells as doublets). Weaker bands at ~45 kDa, very faint bands at ~100 kDa. These bands were absent after exposure to ChREBP blocking peptide, although some faint non-specific banding remained at ~90, ~60, and ~40 kDa. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0023.jpg "Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Mouse liver tissue lysate, 10 ug total protein per lane, probed with CHREBP antibody. Specific bands at ~150 kDa (some wells as doublets). Weaker bands at ~45 kDa, very faint bands at ~100 kDa. These bands were absent after exposure to ChREBP blocking peptide, although some faint non-specific banding remained at ~90, ~60, and ~40 kDa. WB image submitted by a verified customer review.")
![Immunocytochemistry/Immunofluorescence: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - RetSat depletion prevents the glucose-induced nuclear accumulation of ChREBP independent of 13,14-dihydroretinol generation. Hepatocytes were treated with Control or RetSat siRNA overnight. The next morning, cells were incubated with vehicle (DMSO) or 1 uM 13,14-dhretinol for 24 h at the indicated glucose concentrations and mRNA expression of Txnip determined by qPCR. Data are shown as mean +/- s.d., n = 4. Two-way ANOVA with Bonferroni post test revealed significances between low and high glucose (#P < 0.05) and between siControl and siRetSat (*P < 0.05), treatment with 13,14-dhretinol had no effect. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-135-img0021.jpg)
![Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Staining of human colon, epithelium at a 40X magnification.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-135-img0016.jpg)
![Chromatin Immunoprecipitation: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Effects of glucose on ChREBP binding.HepG2 cells were treated with low (2.7 mM) and high (25 mM) glucose for 8 h. Chromatin was isolated and fragmented, and ChIP was performed with control IgG or anti-ChREBP antibody. Validated primers for each gene were used for quantitative real-time PCR. The data presented as fold increase for the signal from anti-ChREBP relative to control IgG. The negative control, Cyclo, showed no enrichment (data not shown). Values represent the mean +/- S.D. of three independent samples. *p<0.005 vs. IgG, #p<0.0001 vs. 2.7 mM glucose with anti-ChREBP. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0022544), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Chromatin-Immunoprecipitation-NB400-135-img0018.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in 20 ug of human hepatocyte lysate using NB400-135. 5-10 second film exposure.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0007.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in liver nuclear extracts from well-fed rats. 7% SDS-PAGE gel, 1:1000 dilution of NB400-135. Photo courtesy of Dr. Uyeda, UT Southwestern University.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0010.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - RetSat depletion in mouse liver reduces protein levels and target gene expression of ChREBP. RetSat and ChREBP protein expression by immunoblotting. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0019.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Protein expression levels of carbohydrate-responsive element-binding protein (ChREBP), in livers of rats receiving normal water (CON), a 13% (w/v) glucose solution (GLU), a 13% (w/v) fructose solution (FRUC), or a 0.4% (w/v) aspartame solution (n = 6 per diet group). All data were normalized to beta-actin expression levels and are expressed relative to the controls (CON). Data are expressed as means +/- SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. CON; +p < 0.05, ++p < 0.01, +++p < 0.001 vs. ASP; p < 0.01, p < 0.001 vs. GLU. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/5/476), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - HeLa cells were fixed for 10 minutes using 10% formalin and permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-ChREBP (NB400-135) at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stained at 1:1000 and detected with an anti-mouse DyLight 550 (Red) at a 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-135-img0017.jpg)
![Immunohistochemistry: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Analysis of CHREBP in mouse liver using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunohistochemistry-NB400-135-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Immunoblot analysis of ChREBP in liver lysates of control and L-Chrebp -/- mice. Aliquots (60 ug of protein) of liver whole-cell lysates were subjected to SDS-PAGE and immunoblot analysis with anti-ChREBP and anti-calnexin antibodies. ChREBP delta denotes a truncated aberrant ChREBP protein present only in lysates prepared from L-Chrebp -/- livers. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29335275/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP Antibody - BSA Free-Knockout Validated-NB400-135-img0024.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Raffinose stimulates transcription of genes involved in epidermal barrier function in HaCaT cells.(a & b) HaCaT cells were treated with vehicle, 1 μM or 10 μM raffinose (Raf), or 1 μM TO901317 (T17) for 24 h. Expressions of transcripts (a) & proteins (b) were analyzed by qRT-PCR or western blotting, respectively. FLG; filaggrin. IVL; involucrin, LOR; loricrin, AQP3; aquaporin3. (c) HaCaT cells were transfected with siGFP control, siLXR alpha , or siLXR beta , & then treated with 1 μM raffinose for 24 h. Expression of proteins was analyzed by western blotting. The original blots are shown in Supplementary Fig. S9. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28266648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415291928.jpg)
![Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - Impaired hepatic SIRT1-FoxO signaling in L-G6pc-/- mice.(A) Western blots & densitometry analysis (n = 5), & quantification of mRNA for hepatic SIRT1 & FoxO3a (n = 8). (B) Hepatic NAD+ levels (n = 9). (C) Western blots & densitometry analysis of PPAR-gamma , PPAR-alpha & beta -actin (n = 5). (D) Immunohistochemical analysis of hepatic ChREBP & quantification of nuclear ChREBP-translocated cells (n = 4). Scale bar, 25 μm. (E) Quantification of mRNA for hepatic Acaca, Fasn & Elovl6 by real-time RT-PCR (n = 6). (F) Western blots of acetylated & total FoxO3a after immunoprecipitation of nuclear extracts using anti-FoxO3a, & quantification of the acetylated FoxO3a/total FoxO3a (n = 5). Data represent the mean ± SEM. *P < 0.05, **P < 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28558013), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415171345.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Expressing recombinant ChREBP beta in Rictor-deficient adipocytes rescues expression of DNL enzymes.Western blot of indicated proteins in differentiated adipocytes with or without Rictor deletion transfected with various rescue constructs that were stably expressed in cells before differentiation. ‘*' indicates ChREBP beta based on molecular weight. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415171318.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Hepatic expression of mRNAs encoding carbohydrate response element-binding protein (ChREBP) (a), liver pyruvate kinase (LPK) (c), & microsomal triglyceride transfer protein (MTTP) (d), & nuclear ChREBP protein (b) in water-control, 10% fructose solution-control, & fructose pair-fed oleanolic acid- (OA-) treated rats at week 10. Animals were administered with OA (25 mg/kg/day) or vehicle (OA: 0 mg/kg, 5% Gum Arabic) by oral gavage daily for 10 weeks. mRNA was determined by real-time PCR. Protein expression was determined by Western blot. Data are means ± SEM (n = 6 each group). *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23737835), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241529337.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR mediate the induction of lipogenesis induced by an oleic acid-rich diet.(A) Hepatic Acly, Acaca, Acacb, Fasn, Elovl6, Scd1 mRNA levels quantified by qPCR. (B) Cytoplasmic protein expression levels of P-ACLY, ACLY, ACC, ELOVL6, SCD1, FASN & beta -ACTIN assayed by Western Blotting. (C) Fads1, Fads2, Elovl5, Gpat, Pnpla3 & Lpk mRNA quantification assayed by qPCR. (D) Srebp-1c & Chrebp mRNA quantification assayed by qPCR. (E) Cytoplasmic & nuclear expression levels of LXR, SREBP-1c & ChREBP assayed by Western Blotting. Data are the mean±SEM of values measured in LXR+/+ & LXR-/- mice fed REF or OLIV diet. a Significant genotype effect. b Significant difference versus REF diet (n = 6 mice per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28732092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241534316.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Analysis of protein levels in livers transfected with GK & GKA456V. Livers excised from mice in postabsorptive state were homogenized & resolved by Western blot. (a, b) Representative blots from three independent experiments. The densitometric analysis is presented (N = 4, *P < 0.05 versus pControl, ***P < 0.001 versus pGKA456V). (c) Liver sections of 5-hour fasted mice injected with pControl, pGK, or pGKA456V were immunostained with Glc6Pase antibody. TO-PRO-3 was used to visualize nuclei. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22194744), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415371929.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - ChREBP knockdown inhibited glycolysis, lipogenesis & p21 in HT29 cells. (A) Inhibited relative mRNA expression of ChREBP alpha & ChREBP beta normalized to B2M after control or ChREBP siRNA transfection for 48 hours. (B) Western-blot of ChREBP, phospho-p53 & p21 & their quantification on the right. beta -actin was served as a loading control. Proteins were extracted from cells transfected with sicontrol & siChREBP after 48 hours. The quantification of western blot was normalized to beta -actin. (C) Decreased relative mRNA expression of glycolytic & lipogenic genes, normalized to B2M. (D) Relative mRNA expression of p53 & p21, normalized to B2M. (E) Relative mRNA expression of cell Cyclins, normalized to B2M. n = 4. *p < 0.05; **p < 0.01; ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32144313), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241528455.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Ligand-activated LXR reduces ChREBP binding to chromatin. (A). Left panels: Local pattern of LXR-ChREBP co-occupancy. Browser view of LXR & ChREBP tracks in the promoter region of Lpk (Pklr), Txnip, Fasn & Scd1. Square brackets indicate the scale maxima of ChIP/input ratios. Arrows indicate the genomic locations of quantitative RT-PCR primers. Right panel: AML12 cells transfected with ChREBP alpha /Mlx gamma & LXR alpha /RXR alpha were treated with DMSO (0.1%) or GW3965 (10 µM) for 18 h. ChREBP or LXR binding to genomic location indicated in the right panels were detected by ChIP using antibodies against ChREBP, LXR or IgG as negative control. Data are presented as mean ± SEM (n = 3–5). Significant differences are shown as * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ChIP-IgG & #p < 0.05, ##p < 0.01, ###p < 0.001 between DMSO & GW3965 groups. ns, not significant. (B). CoIP of LXR alpha & ChREBP alpha , expressed in COS-1 cells cultured in 25 mM glucose, treated with DMSO (0.1%) or GW3965 (1 µM) for 18 h. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or LXR alpha antibodies. One representative western blot is shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416171431.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Induction of hepatic Srebp-1 & carbohydrate response element-binding protein (Chrebp) beta expression by dietary glucose is reduced in LXR alpha −/− mice. (A) Hepatic gene expression of Lxr alpha / beta , Srebp-1, & Chrebp alpha / beta was analyzed by quantitative RT-PCR & normalized to Tbp; (B) Cytosolic & nuclear lysates were immunoblotted with antibodies against LXR, SREBP-1, & ChREBP with alpha -Tubulin & Lamin A as loading controls. Each lane represents independent mice from each group. One representative western blot is shown (n = 3). Data represent the mean ± SEM (n = 5). Significant differences were found using two-way ANOVA followed by Tukey’s multiple comparison test (fasted vs. fructose fed & fasted vs. glucose fed RNA data were analyzed separately). * p < 0.05, ** p < 0.01, *** p < 0.001 compared to fasted. #p < 0.05, ##p < 0.01, ###p < 0.001 compared to LXR alpha +/+ mice. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/7/678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-3102024161891.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Decreased glucose uptake & Chrebp beta -driven DNL is a primary consequence of Rictor loss in adipocytes.(a) Western blots of indicated proteins at different days of differentiation using Rictor iKO primary adipocytes (described in Methods). (b) Oil Red O staining of differentiated adipocytes. (c) The relative mRNA level of ChREBP beta in differentiated cells at various time points. n=3. (d) 2-DG uptake in differentiated adipocytes without or with insulin stimulation. n=3. (e) The C14-glucose-derived FA in differentiated adipocytes. n=3. (f) The C14-glucose derived triglyceride (TAG) in differentiated adipocytes. n=3. (g) Relative glut4 expression in differentiated cells at various time points. n=3. (h) Relative glut4 expression in sWAT. n=8. (i) Glycerol release in differentiated adipocytes under basal & isoproterenol (Iso) stimulation. n=4. (j) Glycerol release in ex vivo pgWAT under basal & isoproterenol stimulation. n=6. Data were analysed by Student's t-test. Values are expressed as mean+s.e.m. *P<0.05; **P<0.01; ***P<0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416163714.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - RetSat controls ChREBP activity & glucose sensing in primary hepatocytes. Primary mouse hepatocytes were treated with Control or RetSat siRNA for 48 h, (a, left) ChREBP mRNA expression determined by qPCR, & RetSat & ChREBP protein levels determined by immunoblotting (a, right). left, Data are shown as mean ± 11s.d., n = 3 independent transfections of hepatocyte cultures from the same mouse. Two independent experiments yielded similar results. b Hepatocytes were treated as described in a & mRNA expression of a selection of known ChREBP target genes visualized in a heatmap. c Primary hepatocytes were depleted of RetSat using two siRNA’s targeting different sites of the RetSat transcript for 48 h, & expression of the indicated genes analyzed by qPCR. Data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two different mice; *P < 0.05 between siControl und siRetSat by one-way ANOVA with Bonferroni post test. An independent experiment yielded similar results. d Hepatocytes treated with Control or RetSat siRNA were transfected with a ChoRE-Luc reporter, exposed to low & high glucose concentrations as indicated, & analyzed for luciferase activity. e Hepatocytes treated with Control or RetSat siRNA were exposed to low & high glucose concentrations as indicated, & mRNA expression determined by qPCR. In d, e, data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two mice; two-way ANOVA with Bonferroni post test revealed significances between low & high glucose concentrations (#P < 0.05) & between siControl & siRetSat (*P < 0.05). An independent experiment yielded similar results Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416165648.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR alpha & ChREBP alpha interact via key activation domains. (A). Top panel: Schematic representation of the ChREBP alpha full-length (FL), ChREBP beta & the low glucose inhibitory domain (LID) protein. Bottom panel: CoIP of LXR alpha & ChREBP alpha , ChREBP beta or LID, expressed in COS-1 cells cultured in 25 mM glucose. The ChREBP expression plasmids were transfected with a DNA ratio of ChREBP alpha :ChREBP beta :LID = 1:6:1, to obtain comparable protein levels. Lysates were immunoprecipitated with ChREBP, FLAG (for LID) or LXR alpha antibodies & input & immunoprecipitated proteins immunoblotted with the same antibodies (n = 3). One representative western blot is shown. LID, low-glucose inhibitory domain; GRACE, glucose-response activation conserved element; bHLH, basic helix-loop-helix domain: ZIP, leucine zipper. (B). Top panel: Schematic representation of the LXR alpha FL & truncations. Bottom panel: CoIP of ChREBP alpha & LXR alpha FL or truncations expressed in COS-1 cells cultured in 25 mM glucose. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or FLAG (for LXR alpha FL & truncations) antibodies. One representative western blot is shown. NTD, N-terminal domain; DBD, DNA-binding domain; LBD, ligand-binding domain. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416175271.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - FXR inhibits glucose-induced proglucagon expression(a) Proglucagon qPCR on cDNA from GLUTag cells starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate (10 mmol L−1), glucose (5.6 mmol L−1) or 2-deoxyglucose (5.6 mmol L−1) media containing DMSO, GW4064 (5 μmol L−1) or CDCA (100 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. ***P≤0.001: effect of GW4064 & CDCA on proglucagon mRNA levels in each medium conditions. §§§P≤0.001: effect of glucose on proglucagon mRNA levels in DMSO, GW4064 & CDCA conditions. (b) Chrebp qPCR on cDNA from FACS-sorted proglucagon-negative & proglucagon-positive cells from the ileum (ileum L−; ileum L+) & colon (colon L−; colon L+) of GLU-VENUS mice (lower panel; n=3) & ChREBP protein expression from cytoplasm & nucleus extract from GLUTag cells (upper panel; performed 3 times). Data are represented as mean +/− SD. Student t-test. *P≤0.05 & **P≤0.01 (c) ChREBP & FXR western-blots after FXR immunoprecipitation on lysates from cytoplasm & nucleus of GLUTag cells treated or not with GW4064 (5 μmol L-1) in presence or not of glucose (5.6 mmol L−1) (performed 2 times). (d) Proglucagon qPCR on cDNA from GLUTag cells electroporated with a siCtrl or siChrebp, starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate 10 mmol L−1 (Glc −) or glucose 5.6 mmol L−1 (Glc +) media supplemented with DMSO or GW4064 (5 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. *P≤0.05 & **P≤0.01: effect of treatments on each transfection condition. §§§P≤0.001: effect of siChrebp in each treatment condition. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms8629), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241616057.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Dietary fructose induces nuclear O-GlcNAc signaling. (A) Simplified schematic overview of the hexosamine signaling pathway including the rate limiting enzyme GFAT & O-GlcNAc transferase (OGT); (B) High-performance liquid chromatography (HPLC) analysis of hepatic UDP-GlcNAc levels. Left panel: Example of a typical running profile w/ or w/out injection of UDP-GlcNAc standard (Std.) is shown. Right panel: Quantification of the HPLC data normalized to protein concentration; (C) Hepatic expression of the Ogt gene & cytosolic & nuclear OGT protein analyzed by quantitative RT-PCR & western blotting/Image J & normalized to Tbp, alpha -tubulin, & Lamin A, respectively. Data represent the mean ± SEM (n = 5); (D) Cytosolic & nuclear lysates immunoblotted w/ anti-O-GlcNAc antibody (RL2) w/ alpha -Tubulin & Lamin A as loading controls. Each lane represents independent mice from each group. One representative western blot is shown (n = 2); (E) Nuclear lysates subjected to wheat germ agglutinin (WGA) beads to precipitate O-GlcNAcylated proteins. WGA enriched samples (upper panel) & input lysates (bottom panel) immunoblotted w/ antibodies detecting O-GlcNAcylated proteins (RL2), LXR & ChREBP. Each lane represents independent mice from experimental groups. Representative western blots are shown (n = 2); (F) ChREBP binding to carbohydrate response element (ChoRE) containing region of the L-pk promoter & negative control sequence (NC) 2216–2288 bp into L-pk gene after ChoRE sequence detected by chromatin immunoprecipitation (ChIP) using antibodies against ChREBP or IgG as a control. Data represent the mean ± SEM (n = 5). Significant differences found using two-way ANOVA followed by Tukey’s multiple comparison test. ** p < 0.01 compared to fasted. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/7/678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416171465.jpg)
![Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - Correction of hepatic G6Pase-alpha deficiency normalizes autophagy.L-G6pc-/- mice were treated with 1 x 1012 vp/kg of rAAV-G6PC at 4 WP & analyzed at 12 WP. (A) Hepatic G6Pase-alpha activity in control (n = 7), L-G6pc-/- (n = 7), & rAAV-treated L-G6pc-/- (AAV/ L-G6pc-/-, n = 8) mice. (B) Liver weights in control (n = 10), L-G6pc-/- (n = 5), & AAV/ L-G6pc-/- (n = 8) mice. (C) The levels of hepatic metabolites in control, L-G6pc-/- & AAV/ L-G6pc-/- (n = 8) mice. (D) Fasting glucose test (FGT) profile of control (n = 13), L-G6pc-/- (n = 6) & AAV/ L-G6pc-/- (n = 8) mice. (E) Western blots of hepatic SIRT1, FoxO3a, LC3B, p62 & beta -actin & densitometry analysis (n = 8). (F) Hematoxylin & eosin (H&E) stained liver sections, & immunohistochemical analysis of hepatic ChREBP & quantification of nuclear ChREBP-translocated cells in control, L-G6pc-/-, & rAAV-treated L-G6pc-/- (AAV/ L-G6pc-/-) mice (n = 4). The insets present higher magnification views. Scale bar, 25 μm. Data represent the mean ± SEM. *P < 0.05, **P < 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28558013), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416175247.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Phf2 expression is increased in the liver of obese patients with benign hepatic steatosis & positively correlates with insulin sensitivity. Human liver biopsies from lean subjects with no fatty liver (NoFL) or obese patients with simple steatosis or NASH were obtained from the ABOS cohort. a Representative Western blot analysis of Phf2, ChREBP, SCD1, Nrf2, Gpx4, & alpha -SMA expression (n = 10 per group). b ChIP experiments for H3K9me2 levels & for the recruitment of ChREBP & the RNA polII at the SCD1 & Nrf2 promoter (n = 10 per group). c MUFA/SFA ratio reflecting SCD1 activity (n = 10 per group). d Expression of Nrf2 & Nrf2-regulated genes (n = 10 per group). e Levels of carbonylated proteins (n = 10 per group). f Expression of coll-Ia1, alpha -SMA, & TIMP-1 (n = 10 per group). All error bars represent mean ± SEM. Statistical analyses were made using Anova, followed by Bonferonni’s test. *Obese with steatosis compared to lean with noFL; P < 0.01. **Obese with steatosis compared to obese with NASH; P < 0.05 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-04361-y), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416163772.jpg)
![Western Blot: DNMT1 Antibody (60B1220.1) [NB100-56519] - Analysis of Dnmt1 in 2102EP (human embryonic carcinoma) in the A) absence and B) presence of immunizing peptide, recombinant human Dnmt1 protein in the C) absence and D) presence of immunizing peptide, NIH 3T3 (mouse embryonic fribroblast) in the E) absence and F) presence of immunizing peptide, and D3 (mouse embryonic stem cell) in the G) absence and H) presence of immunizing peptide using Dnmt1 antibody. this antibody. 5 ug/ml for testing the human cell line and 0.1 ug/ml was used for testing the recombinant protein and the mouse cell lines. ’s goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used for this test.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Western-Blot-NB100-56519-img0003.jpg "Western Blot: DNMT1 Antibody (60B1220.1) [NB100-56519] - Analysis of Dnmt1 in 2102EP (human embryonic carcinoma) in the A) absence and B) presence of immunizing peptide, recombinant human Dnmt1 protein in the C) absence and D) presence of immunizing peptide, NIH 3T3 (mouse embryonic fribroblast) in the E) absence and F) presence of immunizing peptide, and D3 (mouse embryonic stem cell) in the G) absence and H) presence of immunizing peptide using Dnmt1 antibody. this antibody. 5 ug/ml for testing the human cell line and 0.1 ug/ml was used for testing the recombinant protein and the mouse cell lines. ’s goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used for this test.")
![Immunocytochemistry/Immunofluorescence: DNMT1 Antibody (60B1220.1) [NB100-56519] - Dnmt1 antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Antibody dilution of 1:10 was used. Image objective 40x.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Immunocytochemistry-Immunofluorescence-NB100-56519-img0006.jpg)
![Immunohistochemistry-Paraffin: DNMT1 Antibody (60B1220.1) [NB100-56519] - Tissue section of human hepatocellular carcinoma at 1:50 dilution.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Immunohistochemistry-Paraffin-NB100-56519-img0007.jpg)
![Flow Cytometry: DNMT1 Antibody (60B1220.1) [NB100-56519] - An intracellular stain was performed on HeLa cells with DNMT1 [60B1220.1] Antibody NB100-56519AF488 (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.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Flow-Cytometry-NB100-56519-img0010.jpg)
![Flow Cytometry: DNMT1 Antibody (60B1220.1) [NB100-56519] - Analysis of PE conjugate of NB100-56519. An intracellular stain was performed on HeLa cells with DNMT1 antibody (60B1220.1) NB100-56519PE (blue) and a matched isotype control NBP2-27287PE (orange). Cells were fixed with 4% PFA and then permeablized with 0](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Flow-Cytometry-NB100-56519-img0009.jpg)
![Simple Western: DNMT1 Antibody (60B1220.1) [NB100-56519] - Simple Western lane view shows a specific band for Dnmt1 in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Simple-Western-NB100-56519-img0008.jpg)
![Immunoprecipitation: DNMT1 Antibody (60B1220.1) [NB100-56519] - The PCNAS228I mutation differentially affects PCNA binding to PIP box-containing proteins. GST-PIP pull down of His-S-PCNAWT or PCNAS228I. Figure shows Coomassie stained gel of representative pull down (top) and anti-PCNA western blot of the same samples diluted 1:20 (bottom). Amount of 'input' loaded for Coomassie is equivalent to 1%, 'Glut. beads' (Glutathione sepharose 4B beads) is equivalent to 25%. Molecular weight markers are indicated. Image collected and cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S1568786416304013), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Immunoprecipitation-NB100-56519-img0011.jpg)
![Western Blot: DNMT1 Antibody (60B1220.1) - BSA Free [NB100-56519] - WA does not alter DNMTs gene & protein expression(A) Effect of WA on DNMT1, DNMT3A & DNMT3B gene expression in MDA-MB-231 & MCF-7 cells normalized to select housekeeping genes & relative to DMSO-treated MCF-7 sample (2-delta delta Ct) as determined by Human Epigenetic Chromatin Modification Enzyme qPCR Array as previously described. Bars represent DNMT1, DNMT3A & DNMT3B relative mRNA (mean ± SEM) expression of at least two independent experiments. (B) Effect of WA on DNMT1, DNMT3A & DNMT3B protein expression in MDA-MB-231 & MCF-7 cells, as compared to to beta -Actin protein levels. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28467815), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56519_mouse-monoclonal-dnmt1-antibody-60b1220-1-310202415171327.jpg)
![Chromatin Immunoprecipitation: DNMT1 Antibody (60B1220.1) - BSA Free [NB100-56519] - Epigenetic changes & protein binding at Ankrd26 promoter in eAT from mice upon 22 weeks of HFD.ChIP of DNMT1, DNMT3a, DNMT3b (a) & MBD2 (b) binding at Ankrd26 promoter region (−553 bp/−348 bp). (c) MNase for Nuc-2 (−257 bp/−198 bp) & Nuc-1 (−84 bp/−25 bp) occupancy at Ankrd26 promoter. (d) ChIP for acetyl-H4 enrichment at Nuc-2 & Nuc-1. (e) ChIP of RNA Pol II binding at Ankrd26 TSS (+16 bp/+159 bp). (a,b) & (d,e), ChIP enrichment is relative to Input chromatin. (a–e), results are mean ± SD from three independent experiments. **p < 0.01 & ***p < 0.001 vs STD. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep43526), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56519_mouse-monoclonal-dnmt1-antibody-60b1220-1-310202415304276.jpg)
![Western Blot: DNMT1 Antibody (60B1220.1) - BSA Free [NB100-56519] - Verification of the expression of the proteins identified.(A) Validation of the SILAC results of selected proteins in immunoblots of protein extracts from the bladder cancer cells analyzed. The results validated the expression levels of proteins identified by the proteomic approach, including differentially & non-differentially expressed candidates. Antibodies displaying a single predominant band at the expected molecular weights were accepted: & alpha -tubulin, was used as the loading control. GSN, Gelsolin; Cul3, Cullin 3; IPO9. Importin 9; EGFR, Epidermal Growth Factor Receptor; NUP133, Nucleoporin 133; HSP70, Heat Shock Protein 70kDa; MCM6, Minichromosome Maintenance Complex Component 6; RCC1, Regulator of Chromosome Condensation 1; BCAS2, Breast Carcinoma Amplified Sequence 2; DNM, Dynamin; NPM, Nucleophosmin; DCTN, Dynactin; CALR, Calreticulin; MAPK, Mitogen-Activated Protein Kinase; DDX21, DEAD (Asp-Glu-Ala-Asp) box polypeptide 21; CDC2: Cell Division Cycle 2; DNMT1, DNA (cytosine-5)-Methyltransferase 1; MSH6, MutS Homolog 6; RAB14, GTPase Rab14; VDAC, Voltage-Dependent Anion Channel; CK18, Cytokeratin 18; CALD, Caldesmon; CD44, CD44 antigen isoform 1 precursor 2; EZR, Ezrin; MSN, Moesin; ANXA2, Annexin A2; CPNE3, Copine 3; FLNA, Filamin A; CAV1, Caveolin 1. Western Blots were scanned & analyzed using alpha -tubulin as normalizing control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23308193), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56519_mouse-monoclonal-dnmt1-antibody-60b1220-1-3102024165721.jpg)
![Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Simple-Western-NB100-56506-img0010.jpg "Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.")
![Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Analysis in human Jurkat cell lysate at 2 ug/mL. Goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Western-Blot-NB100-56506-img0008.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) [NB100-56506] - Transitional cell carcinoma, urinary bladder, stained with TRF2 antibody (4 ug/mL), peroxidase-conjugate and DAB chromogen. Note specific nuclear staining. Tumor/normal adjacent tissue array slide was used for this test. 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.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunohistochemistry-Paraffin-NB100-56506-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of SNORD17 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0018.jpg)
![Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - Intracellular flow cytometric analysis of TRF2 in 10^6 human Jurkat cells using 0.1 ug of NB100-56506. The shaded histogram represents cells alone, blue represents isotype control and red represents NB100-56506, anti-TRF2.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Flow-Cytometry-NB100-56506-img0001.jpg)
![Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Total protein from mouse 3T3 cells was separated on a 12% 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-TRF2 in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Western-Blot-NB100-56506-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of NEAT1 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0019.jpg)
![Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - An intracellular stain was performed on A431 cells with TRF2 Antibody [4A794.15] NB100-56506 (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).](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Flow-Cytometry-NB100-56506-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Staining of TRF2-bound telomeres in human HeLa cells (Courtesy of Fotiadou, et al, 2004).](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton-X100. The cells were incubated with anti-TRF-2 (4A794.15) conjugated to FITC [NB100-56506F] at 5 ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0017.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - ZBTB48‐dependent loss of MTFP1 phenocopies MTFP1 depletionFluorescence microscopy analysis of the structure & localization of the mitochondrial network in HeLa WT & ZBTB48 KO clones. Mitochondria are marked with the MitoTracker dye (red), & nuclei are counterstained with DAPI (blue). Scale bars represent 20 μm.The same analysis as in (A) for U2OS WT & ZBTB48 KO clones. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28500257), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241534325.jpg)
![Western Blot: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - TRF2 delta B delta M expression induces chromosome end-to-end fusions in all inducible cell lines(A) Immunoblots of MCF-10A, TO, SH-TO & SV-TO cell lines with & without DOX & HEK 293T. After 96 h of DOX treatment, the inducible cell lines expressed the truncated TRF2 delta B delta M protein (50 kDa); in contrast, uninduced cell lines, MCF-10A parental cell line & HEK 293T cells displayed only the endogen TRF2 protein (66 kDa). Lamin B1 was used as loading control. (B) After sustained expression of TRF2 delta B delta M for 96 h there was a significant increase in aberrant metaphases only in TO cells when compared to uninduced matched cells. (C) Nevertheless, the efficacy of the inducible system was validated by the statistical increase of cells with end-to-end fusions in all inducible cell lines. (D) Moreover, a high incidence of fusions per cell was found in all modified cell lines after sustained TRF2 depletion. Data was presented as mean + SEM. (E) Example of TO, SH-TO & SV-TO karyotypes after 96 h of TRF2 delta B delta M expression. Open arrows indicate clonal aberrations in the parental MCF-10A cell line. Insets in the karyotype show rearranged chromosomes stained with centromeric (green) & telomeric (red) PNA probes. Note the presence of telomere FISH signals at the fusion point of chromatid- or chromosome-type end-to-end fusions. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25502), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241682158.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - ZBTB48 ZnF11 necessary to bind to telomeres. Sequence‐specific DNA pull‐downs w/ either telomeric (TTAGGG)/a control sequence (GTGAGT) for FLAG‐ZBTB48 WT, domain deletion constructs for different zinc finger & combinations of deletion constructs w/ ZnF10/11 point mutants. Domain structures indicated - right.Sequence‐specific DNA pull‐downs for FLAG‐ZBTB48 WT & ZnF11 point mutant for telomeric repeat sequences of different phyla (green) & their respective scrambled controls (blue).Protein expression analysis of ZBTB48 by WB for cell lines used. GAPDH serves as a loading control.IF stainings for exogenous FLAG‐ZBTB48 WT & point mutants for ZnF10 & ZnF11 in U2OS cells. The same analysis as in Fig 1E performed & average co‐localization frequencies shown (n = 24–37 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HeLa cells by IF (IF) staining. Image illustrating co‐localization between ZBTB48/FLAG‐ZBTB48 WT (green) & TRF2 (red) as a marker for telomeres is shown w/ DAPI (blue) used as nuclear counterstain. Co‐localization events indicated by white arrows. Quantification of frequency of co‐localization events (right) done after 3D reconstruction of acquired z‐stacks (n = 30 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HeLa 1.3 cells by IF (IF) staining analogous to (E) (n = 30 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HT1080 super‐telomerase cells by IF (IF) staining analogous to (E) (n = 30 cells).Data information: (D–G) Scale bars = 5 μm. Error bars indicate standard deviations, & P‐values based on Student's t‐test.Source data available online for this figure. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/28500257), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241553721.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Samples: Whole cell lysate (15 ug) from HeLa, HEK293T, Jurkat, mouse TCMK-1, and mouse NIH 3T3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-ZEB1 antibody (NBP1-05987) used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes.](http://images.novusbio.com/fullsize/ZEB1-Antibody-Western-Blot-NBP1-05987-img0017.jpg "Western Blot: ZEB1 Antibody [NBP1-05987] - Samples: Whole cell lysate (15 ug) from HeLa, HEK293T, Jurkat, mouse TCMK-1, and mouse NIH 3T3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-ZEB1 antibody (NBP1-05987) used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes.")
![Immunohistochemistry-Paraffin: ZEB1 Antibody [NBP1-05987] - Sample: FFPE section of human breast carcinoma. Antibody: Affinity purified rabbit anti-ZEB1 (NBP1-05987) used at a dilution of 1:1000 (0.2 ug/ml). Detection: DAB.](http://images.novusbio.com/fullsize/ZEB1-Antibody-Immunohistochemistry-Paraffin-NBP1-05987-img0019.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Analysis of ZEB1 in transfected and native mouse cell lysate. Image courtesy of anonymous customer review.](http://images.novusbio.com/fullsize/ZEB1-Antibody-Western-Blot-NBP1-05987-img0003.jpg)
![Immunohistochemistry-Paraffin: ZEB1 Antibody [NBP1-05987] - Analysis of ZEB1 in human liver and spleen tissues. Image courtesy of anonymous customer review.](http://images.novusbio.com/fullsize/ZEB1-Antibody-Immunohistochemistry-Paraffin-NBP1-05987-img0004.jpg)
![Immunohistochemistry-Paraffin: ZEB1 Antibody [NBP1-05987] - Sample: FFPE section of human breast carcinoma. Antibody: Affinity purified rabbit anti-ZEB1 (NBP1-05987) used at a dilution of 1:1000 (0.2 ug/ml). Detection: DAB.](http://images.novusbio.com/fullsize/ZEB1-Antibody-Immunohistochemistry-Paraffin-NBP1-05987-img0018.jpg)
![<b>Independent Antibodies Validation. </b>Immunoprecipitation: ZEB1 Antibody [NBP1-05987] - Detection of human ZEB1 by western blot of immunoprecipitates. Samples: Whole cell lysate (1.0 mg per IP reaction; 20% of IP loaded) from HeLa cells prepared using NETN lysis buffer. Antibodies: Affinity purified rabbit anti-ZEB1 antibody NBP1-05987 used for IP at 3 ug per reaction. ZEB1 was also immunoprecipitated by another rabbit anti-ZEB1 antibody. For blotting immunoprecipitated ZEB1, NBP1-05987 was used at 0.4 ug/ml. Detection: Chemiluminescence with an exposure time of 30 seconds.](http://images.novusbio.com/fullsize/ZEB1-Antibody-Immunoprecipitation-NBP1-05987-img0013.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Lin28a & ETM-related protein expression changed after the knockdown of Zeb1 in mESCs, mEB, GC1, & P19. Western blotting demonstrated that E-cadherin protein expression increased & that Lin28a & Vimentin protein expression decreased in Zeb1-siRNA transfected mESC (panel a), mEB (panel b), GC1 (panel c), & P19 (panel d) cells. Each experiment was performed in triplicate. Abbreviations: NC, negative control; siRNA, small interfering RNA; & WT, wild-type. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35611144), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202415382430.jpg)
![Immunohistochemistry: ZEB1 Antibody [NBP1-05987] - Immunohistochemical staining results of EMT regulators in HG‐PanIN: SNAIL, SLUG, TWIST1, & ZEB1. We categorized & defined three grades: grade 0, <10% positive staining; grade 1, 10%‐50% positive; grade 2, 50%< positive Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30791220), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202415291996.jpg)
![Immunocytochemistry/ Immunofluorescence: ZEB1 Antibody [NBP1-05987] - Location of Zeb1 proteins in mEC lines (mESC, mEB, GC1, & P19). Immunofluorescence analysis was used to determine localization of Zeb1 in mESC, mEB, GC1, & P19 using a Zeb1 antibody (red). Cell nuclei were labeled with Hoechst 33342 (blue). The scale for the measurement bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35611144), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241539712.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Lin28a & ETM-related protein expression changed after the knockdown of Zeb1 in mESCs, mEB, GC1, & P19. Western blotting demonstrated that E-cadherin protein expression increased & that Lin28a & Vimentin protein expression decreased in Zeb1-siRNA transfected mESC (panel a), mEB (panel b), GC1 (panel c), & P19 (panel d) cells. Each experiment was performed in triplicate. Abbreviations: NC, negative control; siRNA, small interfering RNA; & WT, wild-type. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35611144), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241529198.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Lin28a & ETM-related protein expression changed after the knockdown of Zeb1 in mESCs, mEB, GC1, & P19. Western blotting demonstrated that E-cadherin protein expression increased & that Lin28a & Vimentin protein expression decreased in Zeb1-siRNA transfected mESC (panel a), mEB (panel b), GC1 (panel c), & P19 (panel d) cells. Each experiment was performed in triplicate. Abbreviations: NC, negative control; siRNA, small interfering RNA; & WT, wild-type. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35611144), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202415304286.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Zeb1 expression in mESCs, mEB, GC1, & P19. (a) Zeb1 mRNA expression detected by real-time qPCR in mESC, mEB, GC1, & P19 (P < 0.001, data presented as mean value ± SD). (b) Zeb1 protein expression examined by western blot in mESC, mEB, GC1, & P19. Each experiment was performed in triplicate. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35611144), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202415304288.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Lin28a & ETM-related protein expression changed after the knockdown of Zeb1 in mESCs, mEB, GC1, & P19. Western blotting demonstrated that E-cadherin protein expression increased & that Lin28a & Vimentin protein expression decreased in Zeb1-siRNA transfected mESC (panel a), mEB (panel b), GC1 (panel c), & P19 (panel d) cells. Each experiment was performed in triplicate. Abbreviations: NC, negative control; siRNA, small interfering RNA; & WT, wild-type. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35611144), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241528450.jpg)
![Immunocytochemistry/ Immunofluorescence: ZEB1 Antibody [NBP1-05987] - Correlation of the expression of ZEB1 & IL‐6 & other cytokines in various cancers. (A) Correlation analysis of the expression of ZEB1 & cytokines in breast cancer cell lines using data obtained from the Cancer Cell Line Encyclopedia (CCLE). Breast cancer cell lines were selected for the analysis, & each dot represents a cell line. Affymetrix microarray probe IDs for IL6 & IL8 are shown after the gene symbols on the y‐axis. RMA, robust multiarray average. (B) Representative results obtained from the tissue array analysis in Fig. S3. The top panel shows a case that was positive for both nuclear ZEB1 staining (green) & whole‐cell IL‐6 staining (red); scores = 4. The bottom panel shows a case that was negative for both ZEB1 & IL‐6; scores = 1. The samples were counterstained with DAPI to show cell density in the spot. Original magnification: 20 ×. (C) Kaplan–Meier survival curves of breast & lung cancer patients obtained from a public meta‐analysis database & Kaplan–Meier plotter (Gyorffy et al., 2010, 2013). The probability of overall survival of patients as split by median IL6 & IL8 expression is shown. Red: IL6 & IL8 high expression group; black: IL6 & IL8 low expression group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28618162), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241616091.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - SU5402, FGFR1 inhibitor, affects the EMT transcription factors.(A, B) ERK1/2 phosphorylation (p-ERK1/2) determined by immunoblotting in HSC-4 & OTC-04 treated for 30 min w/ 30 ng/ml FGF2 or 30 ng/ml FGF7 in presence of 10% FBS (A) & in TSU & HOC313 cells treated for 1 h w/ 30 ng/ml FGF2 or 30 μM SU5402 in absence of FBS (B). F2, FGF2; F7, FGF7; SU, SU5402. (C) We have previously reported that, after treatment w/ TGF-beta , NMuMG cells underwent EMT w/ the IIIc-isoform of FGFR1[17]. After NMuMG cells pretreated w/ TGF-beta transfected w/ mouse Fgfr1 siRNA or treated w/ SU5402, the cells further incubated in culture medium (CM) from TSU cells. SU, SU5402; siFR1, siRNA against mouse Fgfr1. (D)FGF2 mRNA levels determined by RT-qPCR analyses. The ratio of FGF2 mRNA to GAPDH mRNA in HSC-4 cells indicated as “1”. Each value represents the mean ± SD of triplicate determinations from a representative experiment. Similar results obtained in at least three independent experiments. (E) ERK1/2 phosphorylation (p-ERK1/2) in TSU & HOC313 cells monitored in presence of indicated concentration of SU5402 for 1 h under serum-free culture conditions, followed by immunoblot analysis. (F, G) Expression of indicated genes in TSU cells under serum-free culture conditions determined by RT-qPCR (F) & immunoblot (G) analyses, following treatment w/ 10 μM SU5402. Each value represents the mean ± SD of triplicate determinations from a representative experiment. Similar results obtained from at least three independent experiments. p values determined by Student’s t-test. **p < 0.01. (H) TSU cells treated w/ 10 μM U0126 in absence of FBS subjected to immunoblotting w/ the indicated antibodies. alpha -tubulin used as a loading control (A, B, C, E, G, & H). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31682640), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241616017.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - SU5402, FGFR1 inhibitor, affects the EMT transcription factors.(A, B) ERK1/2 phosphorylation (p-ERK1/2) determined by immunoblotting in HSC-4 & OTC-04 treated for 30 min w/ 30 ng/ml FGF2 or 30 ng/ml FGF7 in presence of 10% FBS (A) & in TSU & HOC313 cells treated for 1 h w/ 30 ng/ml FGF2 or 30 μM SU5402 in absence of FBS (B). F2, FGF2; F7, FGF7; SU, SU5402. (C) We have previously reported that, after treatment w/ TGF-beta , NMuMG cells underwent EMT w/ the IIIc-isoform of FGFR1[17]. After NMuMG cells pretreated w/ TGF-beta transfected w/ mouse Fgfr1 siRNA or treated w/ SU5402, the cells further incubated in culture medium (CM) from TSU cells. SU, SU5402; siFR1, siRNA against mouse Fgfr1. (D)FGF2 mRNA levels determined by RT-qPCR analyses. The ratio of FGF2 mRNA to GAPDH mRNA in HSC-4 cells indicated as “1”. Each value represents the mean ± SD of triplicate determinations from a representative experiment. Similar results obtained in at least three independent experiments. (E) ERK1/2 phosphorylation (p-ERK1/2) in TSU & HOC313 cells monitored in presence of indicated concentration of SU5402 for 1 h under serum-free culture conditions, followed by immunoblot analysis. (F, G) Expression of indicated genes in TSU cells under serum-free culture conditions determined by RT-qPCR (F) & immunoblot (G) analyses, following treatment w/ 10 μM SU5402. Each value represents the mean ± SD of triplicate determinations from a representative experiment. Similar results obtained from at least three independent experiments. p values determined by Student’s t-test. **p < 0.01. (H) TSU cells treated w/ 10 μM U0126 in absence of FBS subjected to immunoblotting w/ the indicated antibodies. alpha -tubulin used as a loading control (A, B, C, E, G, & H). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31682640), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241616067.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Vimentin & ZEB1 protein levels are regulated by OVOL1 & OVOL2 in a human SCC cell line. (A) Relative protein expression levels of OVOL1 & OVOL2 in A431 cells treated with control siRNA, OVOL1 siRNA, or OVOL2 siRNA for 48 h. (Left) Representative blot images & (right) relative expression levels calculated from three independent experiments. (B) Relative protein expression levels of vimentin, ZEB1, & E-cadherin in A431 cells treated with control siRNA, OVOL1 siRNA, or OVOL2 siRNA for 72 h. (Upper) representative blot images & (lower) relative protein expression levels calculated from three independent experiments. Mann–Whitney U-test; error bars represent mean ± standard deviation. Protein expressions are relative to those of beta -actin as a reference. The control siRNA value was set to 1. p-values < 0.05 were assumed to indicate a statistically significant difference; * p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32106476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202416175281.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - PDGFR-alpha / beta promotes sarcoma CSC migration/invasion & anchorage-independent growth.a Western blot analysis of cell adhesion protein N-cadherin & EMT transcription factors Snail, Slug, & Zeb1 in human sarcoma cell lines grown as monolayers & as spheroids. beta -actin was used as the loading control. b Representative images under light microscopy of migration & invasion assays of human sarcoma cell lines grown as monolayers or as spheroids for 24–48 h. Graphs display the number of migrated or invasive cells per field. c Representative light microscopy images of forrmed colonies in soft agar assay of human sarcoma cell lines grown as monolayers or spheroids for 14–20 days. Graph displays the number colonies per field. d Representative images under light microscopy of migration & invasion assays of human sarcoma cell lines grown as monolayers or as spheroids. Spheroid cells were treated with imatinib or DMSO. e Western blot analysis of N-cadherin & EMT-regulating transcription factors in human sarcoma cell lines grown as spheroids & treated with imatinib or DMSO. Experiments in a & e were performed three times with similar results. Bars represent standard deviation. *p < 0.05 compared to Monolayers Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41389-018-0059-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202416182642.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - FGFR1 siRNAs attenuate the malignant phenotypes of cancer cells.(A) mRNA from TSU cells transfected with siRNAs against FGFR1 (siFGFR1) were subjected to conventional RT-PCR to determine the levels of endogenous FGFR1. (B, C, D) After transfection with siFGFR1 in TSU cells, phosphorylation of ERK1/2 (p-ERK1/2) (B), ZEB1 levels (C), & cell morphology (D) were determined. (E) TSU cells transfected with siFGFR1 were subjected to immunofluorescence analyses. Low magnification, 40×; high magnification, 80×. (F, G, H, I) After either treatment with SU5402 or transfection with siFGFR1 in TSU & HOC313 cells, the number of cells & invasive properties were determined under serum-free culture conditions. (J & K) After transfection with siFGFR1c in TSU & HOC313 cells, invasive & migratory properties were determined under serum-free culture conditions in TSU & HOC313 cells, respectively. siNC, non-specific control siRNA. Each value represents the mean ± SD of triplicate determinations from a representative experiment. Similar results were obtained from at least three independent experiments. p values were determined by Student’s t-test. *p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31682640), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202416175241.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - PDGFR-alpha / beta promotes sarcoma CSC migration/invasion & anchorage-independent growth.a Western blot analysis of cell adhesion protein N-cadherin & EMT transcription factors Snail, Slug, & Zeb1 in human sarcoma cell lines grown as monolayers & as spheroids. beta -actin was used as the loading control. b Representative images under light microscopy of migration & invasion assays of human sarcoma cell lines grown as monolayers or as spheroids for 24–48 h. Graphs display the number of migrated or invasive cells per field. c Representative light microscopy images of forrmed colonies in soft agar assay of human sarcoma cell lines grown as monolayers or spheroids for 14–20 days. Graph displays the number colonies per field. d Representative images under light microscopy of migration & invasion assays of human sarcoma cell lines grown as monolayers or as spheroids. Spheroid cells were treated with imatinib or DMSO. e Western blot analysis of N-cadherin & EMT-regulating transcription factors in human sarcoma cell lines grown as spheroids & treated with imatinib or DMSO. Experiments in a & e were performed three times with similar results. Bars represent standard deviation. *p < 0.05 compared to Monolayers Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41389-018-0059-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-310202416163718.jpg)
![Western Blot: ZEB1 Antibody [NBP1-05987] - Nav1.4 protein levels are decreased in muscles from mouse models of SMA. (A) Immunoblot analysis using muscle lysate from P2, P5, P9, & P21 wild type mice. Nav1.4 protein levels increase during postnatal muscle development & form the predominant sodium channel expressed in mature skeletal muscle. GAPDH served as a loading control (N = 3). (B) Representative immunoblot with quantification, showing a decrease in levels of sodium channel Nav1.4 & Nav1.5 in P5 Smn-/-;SMN2 hindlimb muscle compared with controls (N = 3). (C) Quantification of immunoblot analyses in P21 Smn2B/- & control hindlimb muscles revealed a decrease in Nav1.4 levels. Early in postnatal muscle development, the Nav1.5 sodium channel isoform is the most predominant. In P21 Smn2B/- mice, the protein levels of Nav1.5 are higher than in controls (N = 3). (D) The protein level of the Nav1.4 positive regulator, NF1, is not altered in muscles from P21 Smn2B/- mice. Similarly, no change was detected in the protein levels of the Nav1.4 repressor ZEB. (E) Expression of sodium channel Nav1.4 in control sham & denervated samples 1 & 7 days post-denervation was assessed by immunoblot (N = 3). A decrease in the levels of Nav1.4 in muscle was noted at 7 days post-denervation. *, P < 0.05; **, P < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24119341), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05987_rabbit-polyclonal-zeb1-antibody-31020241617522.jpg)
![Immunocytochemistry/Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Caco-2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with YAP1 Antibody (NB110-58358) at 1 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-58358-img0014.jpg "Immunocytochemistry/Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Caco-2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with YAP1 Antibody (NB110-58358) at 1 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.")
![<b>Biological Strategies Validation. </b>Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - LW6 attenuates the accumulation of cellular YAP1 and its nuclear location. After treating PANC-1 cells with LW6 for 12 hours, LW6 decreased the accumulation of YAP1 when compared to Sham treated cells. n =5 per group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31897243/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1 Antibody - BSA Free-Western Blot-NB110-58358-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - YAP/TAZ signaling is not activated by loss of TRAF3. NT, NF2 KO1, and TRAF3 KO1 cells stained for YAP1 and DAPI. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33185187/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-58358-img0015.jpg)
![Immunohistochemistry-Paraffin: YAP1 Antibody - BSA Free [NB110-58358] - YAP1 was detected in immersion fixed paraffin-embedded sections of human placenta using Rabbit Anti-Human YAP1 polyclonal Antibody (Catalog # NB110-58358) at 1:200 for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to nuclear and cytoplasm in trophoblast cells.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-58358-img0010.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Analysis in transfected HEK 293 cell lysate using YAP1 antibody. Observed molecular weight 75 kDa.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Western-Blot-NB110-58358-img0003.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Consequences of ORP5 and ORP8 knockdown on downstream MAPK and PI3K/AKT signaling. Protein from MOH parental, single and double ORP knockdowns as well as cells transfected with empty vector control (pLKO.1) were harvested, and 20 ug was subjected to SDS-PAGE and used for Western blotting. Image collected and cropped by CiteAb from the following publication (//www.life-science-alliance.org/lookup/doi/10.26508/lsa.201900431), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Western-Blot-NB110-58358-img0012.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - YAP1 Antibody [NB110-58358] - Actomyosin activity inhibits beta-catenin- and YAP-driven proliferation of confluent keratinocytes. Effects of cell density and actomyosin activity on YAP phosphorylation. HaCaT cells cultured for 40 h under the sparse and confluent conditions were treated with 100 uM blebbistatin (Blebb) or DMSO (for control) for 6 h, and then lysed and immunoblotted for Ser127-phosphorylated YAP (pYAP), YAP, beta-catenin and actin. Similar results were obtained in two independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep46326), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Western-Blot-NB110-58358-img0011.jpg)
![Simple Western: YAP1 Antibody - BSA Free [NB110-58358] - Simple Western lane view shows a specific band for YAP1 in 0.1 mg/ml of HeLa lysate. Observed molecular weight is 75 kDa. This experiment was performed under reducing conditions using the 12-230kDa separation system.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Simple-Western-NB110-58358-img0007.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human YAP1 Polyclonal Antibody (Catalog # NB110-58358) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for YAP1 at approximately 75 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Knockout-Validated-NB110-58358-img0008.jpg)
![<b>Genetic Strategies Validation. </b>Simple Western: YAP1 Antibody - BSA Free [NB110-58358] - Western lane view shows lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. A specific band was detected for YAP1 at approximately 81 kDa (as indicated) using 50 ug/mL of Rabbit Anti-YAP1 Polyclonal Antibody (Catalog # NB110-58358). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Knockout-Validated-NB110-58358-img0009.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Yap deficiency suppresses cell proliferation in vivo & in vitro. (A-F) The Ki67 positive ratio of lens epithelial cells decreased in Yap-deficient mice at different stages (arrowheads indicate Ki67 positive cells). (G) The relative number of Ki67 positive lens epithelial cells (number of Ki67 positive lens epithelial cells / lens epithelium area). The data are shown as mean ± S.E.M. (Student’s t-test, *P<0.05, **P<0.01, n=10). (H-I) Knockdown efficiency of Yap in alpha TN4 cell using siRNA. (J-K) Cell viability & growth assay revealed that proliferation was downregulated in Yap knockdown alpha TN4 cells. The data are shown as mean ± S.E.M. (Two-way RM ANOVA, **P<0.01, n=5). Scale bars: 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-31020241535689.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Synergistic effect of LW6 & metformin on YAP1. 80 µM LW6, 20 mM metformin (Met) & the combinational treatment metformin plus LW6 increased phosphorylation of YPA1 at serine 127 & decreased cellular YAP1 concentration after treating cells for 24 hours (A). Moreover, this combinational therapy attenuated the nuclear localization of YAP1 compared to Sham treated cells (B). In addition, lysophosphatidic acid (LPA) & the phosphorylation deficient mutant YAP1-S127A stimulate cell migration of 6606PDA cells (C & D). n = 2 per group for A, n = 3 per group for B, n = 7 per group for C, n = 9 per group for D. Bar = 5µm. Arrows point to nuclei. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31897243), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202415371934.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Consequences of ORP5 & ORP8 knockdown on downstream MAPK & PI3K/AKT signaling.Protein from BxPC-3, PANC-1, MiaPaCa-2, & MOH parental, single & double ORP knockdowns as well as cells transfected with empty vector control (pLKO.1) were harvested, & 20 μg was subjected to SDS–PAGE & used for Western blotting. EGFR, MAPK, & PI3K signaling were assayed as pEGFR, ppERK, & pAKT levels, respectively. Amplification of YAP-1 was also evaluated. Total ERK, total AKT, & beta -actin levels were used as loading controls. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31451509), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202415291931.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Ajuba depletion induces beta -catenin translocation & Cyclin D1 expression in HCC cell lines. a Immunoblotting with specific antibodies against Ajuba, E-cadherin, beta -catenin, Cyclin D1, YAP, TAZ & CYR61 in Ajuba-depleted BEL7402 & HepG2 cells. GAPDH was used as a loading control. The ratios of expression E-Cadherin to their corresponding GAPDH are represented. b Ajuba-depleted HCC cells were fixed for immunofluorescence & stained for beta -catenin protein (green) & DAPI (blue). Representative merged images are also shown for fluorescence signals. Scale bar = 25 μm. c Correlation of Ajuba expression with OS in HCC. Low expression of Ajuba was associated with worse OS compared to high expression of Ajuba. Kaplan-Meier curves & log-rank test were used to evaluate OS. P < 0.05 was considered significant. d, e Representative images & quantification of migration & invasion of Ajuba-depleted (d) or Ajuba-overexpressing (e) HCC cells. Scale bar = 200 μm. HCC, hepatocellular carcinoma. f Expression in response to the overexpression of constructs of Ajuba-Myc was examined by IB, the ratios of expression Ajuba to their corresponding GAPDH are represented. Data are presented as Mean ± SEM from three independent experiments (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30041665), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235517.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - YAP & TAZ expression at high density & during chondrogenic differentiation of human synovial MSCs. (A) YAP & pYAP expression in human synovial membrane-derived (hSM-)MSCs in monolayer at low (L) & high (H) density detected by immunofluorescence staining, shown without (i) & with sytox green nuclear counterstain (ii). (B) YAP & pYAP expression in hSM-MSCs in monolayer at low (L) & high (H) density detected by western blotting with beta -actin as loading control. (C, D) Expression of YAP & TAZ (C) & their target genes CTGF & CYR61 (D) in hSM-MSCs immediately prior to (0 h) or 24 h after plating in micromass culture, determined by quantitative RT-PCR. Data was normalised to GAPDH expression, & is shown as mean ± standard deviation (SD) (three donors) relative to pre-seeding (0 h) control. *P <0.05; **P <0.01; ***P <0.001. (E) Expression of YAP & TAZ in hSM-MSCs after 6 days of treatment with 10 ng/ml TGF-beta 1 or vehicle only in micromass culture to induce chondrogenic differentiation, determined by quantitative RT-PCR. Data was normalised to GAPDH expression, & is shown as mean ± SD (five donors) relative to vehicle-treated control. *P <0.05. (F) Detection of YAP by western blotting during chondrogenic differentiation induced by TGF-beta 1 with detection of beta -actin as loading control. MSC, mesenchymal stromal/stem cell; pYAP, phosphorylated YAP; RT-PCR, reverse transcription PCR; TAZ, transcriptional co-activator with PDZ-binding motif; TGF, transforming growth factor; YAP, Yes-associated protein. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26025096), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235539.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Expression of spcCre is associated with loss of YAP in SOX9+ distal airways.(A–D) Immunostaining of lung sections collected from Yapf/f; spcCre/+ mice at 13.5 days post coitus (dpc). SOX2 expression marks the proximal airway, while the distal airway is distinguished by SOX9 expression (not shown). High levels of spcCre expression were largely confined to the distal airway, where spcCre expression in a given epithelial cell was correlated with loss of YAP immunoreactivity (e.g. arrowheads in D). (E–H) Immunostaining of lung sections collected from Yapf/f; spcCre/+ mice at 14.5 dpc. Only distal airways are shown. YAP was lost mainly in distal airways in Yapf/f; spcCre/+ mice while sporadic loss of YAP was found in the proximal airway. Loss of YAP was most apparent in the more distal part (arrow in H) of the distal airway, while residual YAP could be found in the more proximal part of the distal airway. Together, these results suggest that lung cyst formation in distal airways of Yapf/f; spcCre/+ mice is due to loss of YAP in the distal airway. Scale bar = 25 μm for A–D; E–H.DOI://dx.doi.org/10.7554/eLife.21130.012 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235526.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - The expression patterns of Yap & GFAP-Cre recombinase in postnatal mouse eyes. (A) Schematic of a transverse section of mouse eye. (B-C) Immunostaining with anti-Yap antibody (green) on frozen eye sections at different ages. Nuclei were counterstained with DAPI (blue). Yap staining was detected in scattered cells within the INL (arrowheads) & GCL of the retina & the lens epithelium (arrows). (D) Cre recombinase (red) was expressed in the lens epithelium & INL, GCL of retina in frozen eye sections of Tomatof/+; GFAP-Cre mice at P14. Nuclei were counterstained with DAPI (blue). LE, lens epithelium; TZ, transitional zone; RPE, retinal pigment epithelium; OS, outer segment; IS, inner segment; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer. Scale bars: 25 μm (B-C), 100 μm (D). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235548.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - YAP & phospho-YAP are detected in both the proximal & distal airways during lung development.(A–H) Immunostaining of lung sections collected from wild-type mice at 13.5 days post coitus (dpc). The proximal airway is marked by SOX2 expression, while the distal airway is distinguished by SOX9 expression (not shown). Nuclear YAP can be frequently found in both SOX2+ & SOX9+ domains. Similarly, phospho-YAP at S112 (pYAP) could be detected in both the proximal & distal airways. pYAP levels were, in general, higher in the proximal than distal epithelium but pYAP levels varied significantly from cell to cell in both the proximal & distal airways. Representative cells with higher levels of pYAP (arrowhead) are indicated in (B,F). In many cells, low levels of pYAP were associated with the presence of nuclear YAP. This is consistent with a model in which pYAP is sequestered by 14-3-3 proteins in the cytoplasm & degraded but also indicate a dynamic shuttling & distribution of YAP along the entire airway epithelium. Similar results were obtained for lungs collected at 12.5 dpc. Scale bar = 7.5 μm for A–H.DOI://dx.doi.org/10.7554/eLife.21130.005 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-31020241623554.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Expression of Nkx2.1Cre is associated with loss of YAP in the upper lobes.(A–D) Immunostaining of lung sections collected from Yapf/f; Nkx2.1Cre/+ mice at 14.5 days post coitus (dpc). SOX2 expression marks the proximal airway, while the distal airway is distinguished by SOX9 expression (not shown). YAP was lost mainly in the upper lobe in Yapf/f; Nkx2.1Cre/+ lung. Loss of YAP was more apparent in the distal airway, while loss of YAP was sporadic in the proximal airway. Lung cyst formation was primarily observed in the distal airway. The boxed region in (B) indicates areas shown in (C,D). Scale bar = 250 μm for A,B; 250 μm for C,D. Sox2 expression was present in sporadic Yap-deficient cells in the transition zone induced by Sox9Cre, spcCre or Nkx2.1Cre. This suggests that Sox2 expression is not controlled by YAP.DOI://dx.doi.org/10.7554/eLife.21130.013 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235520.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Active nuclear YAP is distributed throughout the mouse lung epithelium during development.(A–P) Immunostaining of lung sections collected from wild-type mice at 11.5 & 12.5 days post coitus (dpc). The boxed region in (L) indicates areas shown in (N–P). The proximal airway is marked by SOX2 expression, while the distal airway is distinguished by SOX9 expression. Nuclear YAP can be frequently found in both SOX2+ & SOX9+ domains & is not restricted to the junction (the ‘transition zone’) between SOX2+ & SOX9+ domains. Representative cells with nuclear YAP (arrowhead) are indicated in (E,P). YAP immunoreactivity is completely absent in the epithelium (but present in the mesenchyme) of Yapf/f; ShhCre/+ mice (M), demonstrating the specificity of YAP antibodies used in this study. Immunofluorescence & immunohistochemistry yielded the same results (data not shown for immunohistochemistry). (Q–R) Whole-mount immunostaining of wild-type & Yap mutant lungs at 11.5 dpc. Distinct domains of SOX2 were discerned in the absence of YAP. Scale bar = 10 μm for A–J; 25 μm for K, L; 10 μm for N–P; 50 μm for Q, R.DOI://dx.doi.org/10.7554/eLife.21130.004 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235530.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - The expression patterns of Yap & GFAP-Cre recombinase in postnatal mouse eyes. (A) Schematic of a transverse section of mouse eye. (B-C) Immunostaining with anti-Yap antibody (green) on frozen eye sections at different ages. Nuclei were counterstained with DAPI (blue). Yap staining was detected in scattered cells within the INL (arrowheads) & GCL of the retina & the lens epithelium (arrows). (D) Cre recombinase (red) was expressed in the lens epithelium & INL, GCL of retina in frozen eye sections of Tomatof/+; GFAP-Cre mice at P14. Nuclei were counterstained with DAPI (blue). LE, lens epithelium; TZ, transitional zone; RPE, retinal pigment epithelium; OS, outer segment; IS, inner segment; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer. Scale bars: 25 μm (B-C), 100 μm (D). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-31020241623552.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical analysis in non-GIST STS representing negative, and score 1-3 of Carbonic Anhydrase IX/CA9, GLUT-1, HIF-1 alpha, and HIF-2 alpha/EPAS1. non-GIST STS: non-gastrointestinal stromal tumor soft-tissue sarcomas, Carbonic Anhydrase IX/CA9: carbonic anhydrase IX, GLUT-1: glucose transporter-1, and HIF-1/2alpha: hypoxia induced factor 1/2alpha. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/sarcoma/2012/541650/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-NB100-131-img0030.jpg "Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical analysis in non-GIST STS representing negative, and score 1-3 of Carbonic Anhydrase IX/CA9, GLUT-1, HIF-1 alpha, and HIF-2 alpha/EPAS1. non-GIST STS: non-gastrointestinal stromal tumor soft-tissue sarcomas, Carbonic Anhydrase IX/CA9: carbonic anhydrase IX, GLUT-1: glucose transporter-1, and HIF-1/2alpha: hypoxia induced factor 1/2alpha. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/sarcoma/2012/541650/), licensed under a CC-BY license.")
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Histologically distinct cell types in hemangioblastomas do not arise from a common ancestral clone. Representative images of sample SH-0622 acquired at 400x of (a) H + E and IHC for (b) HIF1-alpha reveal heterogenous cell types in this tumor characterized by a rich vascular network. Arrowheads indicate that the stromal cells demonstrate increased cytoplasmic staining for HIF1-alpha and VEGF, whereas the double arrowheads highlight PDGFR-beta protein restricted to vascular endothelium. Scale bar is 25 um. Image collected and cropped by CiteAb from the following publication (//www.actaneurocomms.org/content/2/1/167), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-NB100-131-img0029.jpg)
![Simple Western: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Image shows a specific band for HIF-1 alpha in 0.5 mg/mL of Hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Simple-Western-NB100-131-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Detection of HIF-1 alpha (red dye 568) in a cultured raw mouse macrophage cell line, using NB100-131. Photos courtesy of Susan Alexander and Hattie Gresham, PhD.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunocytochemistry-Immunofluorescence-NB100-131-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Detection of HIF-1 alpha (red dye) in a cell cytospin from a lavage of a murine skin pouch infected with S. aureus. 100X magnification. Blue: DAPI nuclear staining.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunocytochemistry-Immunofluorescence-NB100-131-img0016.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Analysis of a FFPE mouse kidney tissue section using HIF-1 alpha antibody clone ESEE122 at 1ug/mL concentration. The detection was performed using X-cell plus universal HRP polymer detection system with Vector SG chromagen substrate. Image courtesy of a product review by Steven Grover.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-Paraffin-NB100-131-img0019.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical staining of HIF-1 alpha in normal renal tissue (A) and clear cell renal cell carcinoma (CCRCC) (D). A homogeneous cytoplasmic staining of tubular cells and weak staining in glomerules was observed with HIF-1 alpha (A). In CCRCC, HIF-1 alpha immmunoreactivity was nuclear and/or cytoplasmic (D), while it was perimembranous and/or diffuse cytoplasmic for VEGF-A and VEFG-C (E and F). (magnification x200). Image collected and cropped by CiteAb from the following publication (//www.jeccr.com/content/28/1/40), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-NB100-131-img0031.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Analysis of HIF-1 alpha in paraffin-embedded mouse kidney tissue section using anti-HIF-1 alpha antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-Paraffin-NB100-131-img0021.jpg)
![<b>Biological Strategies Validation. </b>Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Nuclear HIF-1 alpha protein expression. Xenografts were established in female nude mice (BALB c[nu/nu]) by subcutaneous injection of head and neck squamous cell carcinoma cell lines UT-SCC-2 (UT-2) and UT-SCC-14 (UT-14). Cetuximab (1 mg/injection) or PBS was administered by intraperitoneal injection at day 10, 14, and 17. A tissue microarray was constructed from tumours harvested at day 21, and the expression of nuclear HIF-1 alpha was evaluated by immunohistochemistry (IHC) in untreated controls and cetuximab-treated tumour specimens. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28756482/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-NB100-131-img0033.jpg)
![Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Detection of HIF-1 alpha (red dye) in a cell cytospin from a lavage of a murine skin pouch infected with S. aureus, using NB100-131. Blue: DAPI nuclear staining. Image courtesy of Susan Alexander and Hattie Gresham, PhD.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunocytochemistry-Immunofluorescence-NB100-131-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Detection of HIF-1 alpha (red dye 568) in a cultured raw mouse macrophage cell line. 100X magnification. Image courtesy of Susan Alexander and Hattie Gresham, PhD.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunocytochemistry-Immunofluorescence-NB100-131-img0007.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Negative control stain of human placenta (from sea level) using mouse IgG at 1:100. 4uM paraffin-embedded section.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-Paraffin-NB100-131-img0018.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Analysis of a FFPE tissue section of human renal cancer xenograft using HIF-1 alpha antibody (NB100-131 Lot 83115) at 1:200 dilution. The antibody generated a strong cytoplasmic staining mainly in the cancer cells. Only a fraction of cells depicted nuclear staining, while weak to negligible positivity was seen in the tumor stromal cells.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-Paraffin-NB100-131-img0024.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - HIF-1 alpha staining in hypoxia-induced human placenta.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-NB100-131-img0025.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Representative immunohistochemical expression for HIF-1alpha, c-Met, CA9 and GLUT1. HIF-1alpha is stained in cytoplasm shown with no staining in normal cervix (A), weak staining intensity in high grade CIN (B), and strong staining intensity in squamous cell carcinoma (C). Scale bar: 50 um. Image collected and cropped by CiteAb from the following publication (//www.translational-medicine.com/content/11/1/185), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-ESEE122-Immunohistochemistry-Paraffin-NB100-131-img0032.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Histologically distinct cell types in hemangioblastomas do not arise from a common ancestral clone. “Representative images of sample SH-0622 acquired at 400x of (a) H + E & IHC for (b) HIF1-alpha , (c) VEGF, & (d) PDGFR-beta reveal heterogenous cell types in this tumor characterized by a rich vascular network. Arrowheads indicate that the stromal cells demonstrate increased cytoplasmic staining for HIF1-alpha & VEGF, whereas the double arrowheads highlight PDGFR-beta protein restricted to vascular endothelium. Scale bar is 25 μm. Image collected & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/s40478-014-0167-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-31020241534345.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical analysis in non-GIST STS representing negative, & score 1–3 of CAIX, GLUT-1, HIF-1 alpha , & HIF-2 alpha . non-GIST STS: non-gastrointestinal stromal tumor soft-tissue sarcomas, CAIX: carbonic anhydrase IX, GLUT-1: glucose transporter-1, & HIF-1/2 alpha : hypoxia induced factor 1/2 alpha . Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22454562), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-310202415371952.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Digital image analysis of cytoplasmic & membranous staining. Cytoplasmic HIF-1 alpha staining is shown (A) & automated image analysis utilizing TissueIA recognizes cytoplasmic HIF-1 alpha staining highlighted in green color (B). CA9 is shown in membranous staining (C) & automated image analysis determines membranous CA9 staining highlighted in green color (D). The output from the algorithm returns a number of quantitative measurements for intensity & percentage of positive staining present. Scale bar: 100 μm. Image collected & cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-185), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-31020241534362.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical staining of HIF-1 alpha , VEGF-A & VEGF-C in normal renal tissue (A-C) & clear cell renal cell carcinoma (CCRCC) (D-F). A homogeneous cytoplasmic staining of tubular cells & weak staining in glomerules was observed with HIF-1 alpha (A), while VEGF-A & VEGF-C were positive in tubular cells, glomerular mesangium & interstitial macrophages (B & C). In CCRCC, HIF-1 alpha immmunoreactivity was nuclear and/or cytoplasmic (D), while it was perimembranous and/or diffuse cytoplasmic for VEGF-A & VEFG-C (E & F). (magnification ×200). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19302703), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-310202415371953.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Positive immunohistochemical staining for (A) VEGF, (B) HIF-1 alpha , (C) Dll4 (tumor cells), (D) Dll4 (endothelial cells), & (E) CD31 (for microvessel counting, ×200 magnification). Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/or.2012.2075), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-310202415384140.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Immunohistochemical staining of HIF-1 alpha , VEGF-A & VEGF-C in normal renal tissue (A-C) & clear cell renal cell carcinoma (CCRCC) (D-F). A homogeneous cytoplasmic staining of tubular cells & weak staining in glomerules was observed with HIF-1 alpha (A), while VEGF-A & VEGF-C were positive in tubular cells, glomerular mesangium & interstitial macrophages (B & C). In CCRCC, HIF-1 alpha immmunoreactivity was nuclear and/or cytoplasmic (D), while it was perimembranous and/or diffuse cytoplasmic for VEGF-A & VEFG-C (E & F). (magnification ×200). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19302703), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-310202415363744.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Representative immunohistochemical expression for HIF-1 alpha , c-Met, CA9 & GLUT1. HIF-1 alpha is stained in cytoplasm shown with no staining in normal cervix (A), weak staining intensity in high grade CIN (B), & strong staining intensity in squamous cell carcinoma (C). c-Met (D-F), CA9 (G, H) & GLUT1 (I) shows cell membranous staining. Representative c-Met expression in cervical samples shown with no staining in normal cervix (D), weak membranous staining intensity in squamous cell carcinoma (E) & strong intensity in squamous cell carcinoma (F). CA9 expression showing moderate intensity staining in carcinoma in situ (CIS) (G) & strong staining in adenocarcinoma (H). GLUT1 expression showing strong intensity in squamous cell carcinoma (I). Scale bar: 50 μm. Image collected & cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-185), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-310202415532087.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody (ESEE122) [NB100-131] - Representative immunohistochemical expression for HIF-1 alpha , c-Met, CA9 & GLUT1. HIF-1 alpha is stained in cytoplasm shown with no staining in normal cervix (A), weak staining intensity in high grade CIN (B), & strong staining intensity in squamous cell carcinoma (C). c-Met (D-F), CA9 (G, H) & GLUT1 (I) shows cell membranous staining. Representative c-Met expression in cervical samples shown with no staining in normal cervix (D), weak membranous staining intensity in squamous cell carcinoma (E) & strong intensity in squamous cell carcinoma (F). CA9 expression showing moderate intensity staining in carcinoma in situ (CIS) (G) & strong staining in adenocarcinoma (H). GLUT1 expression showing strong intensity in squamous cell carcinoma (I). Scale bar: 50 μm. Image collected & cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-185), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-131_mouse-monoclonal-hif-1-alpha-antibody-esee122-31020241553723.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Head and neck cancer cells have different expression levels of the core clock protein BMAL1. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Western-Blot-NB100-2288-img0021.jpg "Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Head and neck cancer cells have different expression levels of the core clock protein BMAL1. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.")
![Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Analysis of BMAL1 in mouse cerebral cortex (left: wt, right: Bmal1 KO) using anti-BMAL1 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Chromatin-Immunoprecipitation-NB100-2288-img0018.jpg)
![<b>Biological Strategies Validation. </b>Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Inhibition of mTOR signaling with Rapamycin rescues PTEN-driven accumulation of BMAL1A. Tissue samples and graphic show BMAL1 in K14cre PtenF/F mice and control (arrows). Note a significant amount of BMAL1 expression in PTEN mutant mice. K14cre PtenF/F mice and control littermates received Rapamycin or vehicle every other day for 15 days. Rapamycin treatment reduces the expression of nuclear BMAL1 in K14cre PtenF/F mice (arrowhead) (*** p0.05). Scale bars -30um. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2288-img0024.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534364.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415171349.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415304255.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241538245.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534379.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534315.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241535633.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1A. Head & neck cancer cells have different expression levels of the core clock protein BMAL1. B. Immunofluorescence assay depicts accumulation of ROS (green channel) & BMAL1 (red channel) upon oxidation. C. & D. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p<0.05, **p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415363747.jpg)
![Immunocytochemistry/ Immunofluorescence: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415523930.jpg)
![Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Astrocyte Bmal1 regulates genes with conflicting effects on A beta deposition. (A) Topro, GFAP, & BMAL1 staining in CA1 hippocampus of 4-month-old BMAL1 aKO; APP/PS1-21 mice & Cre- controls (scale bar = 100 µm). Arrows indicate astrocyte nuclei quantified as indicated by Topro nuclei surrounded by GFAP positivity. Blue circles indicate nuclei quantified as BMAL1 negative. Quantification of astrocytes counted as BMAL1- or BMAL1+ is shown on the right. n = 5 mice per group, **** = p < 0.0001 by two-way ANOVA with Sidak multiple comparisons test. (B) Heatmap of Fluidigm qPCR analysis of 20 genes involved in the circadian clock, glial activation, & Alzheimer’s Disease in cortex from Aldh1l1-CreERT2; Bmal1fl/fl mice & Cre- controls with or without APP/PS1-21 or APPNL-G-F/wt (n = 6–8 mice per group). Two-way ANOVA analysis: c = significant main effect of Cre genotype, m = main effect of A beta model, c*m = interaction effect of cre & A beta model, - = no significance (all p < 0.05). (C) Individually plotted genes from A. * = p < 0.05, ** = p < 0.005, *** = p < 0.0005 by two-way ANOVA with Sidak multiple comparisons test. Panel B was made using GraphPad Prism version 9.2 (//www.graphpad.com). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35110643), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415525251.jpg)
![ELISA: Human, Mouse, Rat RelA/NFkB p65 ELISA Kit (Colorimetric) [NBP2-29661] - Standard curve using the internal RelA standard.](http://images.novusbio.com/fullsize/Human-Mouse-Rat-RelA-NFkB-p65-ELISA-Kit-Colorimetric-ELISA-NBP2-29661-img0004.jpg "ELISA: Human, Mouse, Rat RelA/NFkB p65 ELISA Kit (Colorimetric) [NBP2-29661] - Standard curve using the internal RelA standard.")
![ELISA: Human, Mouse, Rat RelA/NFkB p65 ELISA Kit (Colorimetric) [NBP2-29661] - Nuclear translocation of NF-kB p65 with LPS in Jurkat cells. Jurkat cells, grown to a density of 2X10(6) cells/ml, were treated with LPS (15 ug/ml). The cells were harvested at various indicated time points, and cell lysates were tested in Western analysis using NB100-56712 and also in this ELISA Kit.](http://images.novusbio.com/fullsize/Human-Mouse-Rat-RelA-NFkB-p65-ELISA-Kit-Colorimetric-ELISA-NBP2-29661-img0005.jpg)
![ELISA: Human, Mouse, Rat RelA/NFkB p65 ELISA Kit (Colorimetric) [NBP2-29661] - Immunofluorescence indicates NF-kB p65 subunit was expressed exclusively in AA-G groups and AST-G cytoplasm. High glucose stimulation impact on TSMCs in NF-kB pathway. (A) NF-kB p65 protein subunit expression in TSMCs in each group. (B) NF-kB p65 subunit immunofluorescence. Each number denotes different subunits. Alexa 488 green served as secondary antibodies.Citation: Hara K, Hamada C, Wakabayashi K, Kanda R, Kaneko K, Horikoshi S, et al. (2017) Scavenging of reactive oxygen species by astaxanthin inhibits epithelial-mesenchymal transition in high glucose-stimulated mesothelial cells. PLoS ONE 12(9): e0184332. //doi.org/10.1371/journal.pone.0184332](http://images.novusbio.com/fullsize/Human-Mouse-Rat-RelA-NFkB-p65-ELISA-Kit-Colorimetric-ELISA-NBP2-29661-img0006.jpg)
![Hydralazine enhances NRF2 signaling in SH-SY5Y cells. c Hydralazine reduced the interaction between NRF2 and KEAP1. Interactions were measured by reciprocal Co-IPs followed by western blot analysis. *p 0.05). n = 5–6/group. * P Sample: Neuro2A cells were fixed in 4% paraformaldehyde at RT for 15 min.Green: Nrf2 stained by Nrf2 antibody [N2C2], Internal (NBP1-32822) diluted at 1:1000.](http://images.novusbio.com/fullsize/nbp1-32822_rabbit-polyclonal-nrf2-antibody-91020242021994.jpg "Hydralazine enhances NRF2 signaling in SH-SY5Y cells. c Hydralazine reduced the interaction between NRF2 and KEAP1. Interactions were measured by reciprocal Co-IPs followed by western blot analysis. *p 0.05). n = 5–6/group. * P Sample: Neuro2A cells were fixed in 4% paraformaldehyde at RT for 15 min.Green: Nrf2 stained by Nrf2 antibody [N2C2], Internal (NBP1-32822) diluted at 1:1000.")
![Immunohistochemistry-Paraffin: Nrf2 Antibody [NBP1-32822] - Nrf2 antibody [N2C2], Internal detects Nrf2 protein at cytoplasm and nucleus by immunohistochemical analysis.Sample: Paraffin-embedded human breast carcinoma.Nrf2 stained by Nrf2 antibody [N2C2], Internal (NBP1-32822) diluted at 1:500.Antigen Retrieval: Citrate buffer, pH 6.0, 15 min](http://images.novusbio.com/fullsize/nbp1-32822_rabbit-polyclonal-nrf2-antibody-910202420115018.jpg)
![Immunocytochemistry/ Immunofluorescence: Nrf2 Antibody [NBP1-32822] - Nrf2 antibody [N2C2], Internal detects Nrf2 protein at nucleus by immunofluorescent analysis.Sample: HeLa cells were fixed in 4% paraformaldehyde at RT for 15 min.Green: Nrf2 stained by Nrf2 antibody [N2C2], Internal (NBP1-32822) diluted at 1:1000.Red: phalloidin, a cytoskeleton marker, diluted at 1:200.Scale bar= 10 um.](http://images.novusbio.com/fullsize/nbp1-32822_rabbit-polyclonal-nrf2-antibody-9102024202465.jpg)
![<b>Orthogonal Strategies Validation. </b>Untreated (-) and treated (+) HepG2 whole cell extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with Nrf2 antibody [N2C2], Internal (NBP1-32822) diluted at 1:2000. The HRP-conjugated anti-rabbit IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nbp1-32822_rabbit-polyclonal-nrf2-antibody-western-blot-1411202518393121.jpg)
![Western Blot: SREBP1 Antibody (2A4) [NB600-582] - Hepatic SREBP1c and SREBP2 protein abundance in C57BL/6 mice assigned to a high-fat (HF) or a high-fat/exercise (HF + EX) group for 8 weeks. Cytosolic and nuclear SREBP1c abundance. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/908048/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Western-Blot-NB600-582-img0004.jpg "Western Blot: SREBP1 Antibody (2A4) [NB600-582] - Hepatic SREBP1c and SREBP2 protein abundance in C57BL/6 mice assigned to a high-fat (HF) or a high-fat/exercise (HF + EX) group for 8 weeks. Cytosolic and nuclear SREBP1c abundance. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/908048/), licensed under a CC-BY license.")
![Western Blot: SREBP1 Antibody (2A4) [NB600-582] - Analysis of whole cell lysate from HeLa cells showing a single specific band for the expression of SREBP1 precursor protein (~120 kDa).](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Western-Blot-NB600-582-img0002.jpg)
![Simple Western: SREBP1 Antibody (2A4) [NB600-582] - Lane view shows a specific band for SREBP1 in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Simple-Western-NB600-582-img0003.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: SREBP1 Antibody (2A4) [NB600-582] - KO and OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, and WT Bel-7402 cells. Data were expressed as mean -/+ standard error of the mean. *P < 0.05, **P < 0.01, and ***P < 0.001 vs. WT group, respectively.](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Knockout-Validated-NB600-582-img0005.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the expression of Nrf2‐related signalling proteins in OA (660 μmol/L) & PA (330 μmol/L)‐induced HepG2 cells. GEN was added into HepG2 cells prior 1 h to stimulation of OA & PA for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm was detected by Western blot. (D & E) Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta & AMPK beta was detected by Western blot. F‐H, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control Group; *P < .05 & **P < .01 vs OA & PA Group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-31020241534375.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - KO & OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. (A) Total cellular TG content of SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (B) HPLC-MS determination of the SFAs to MUFAs ratios (palmitic acid to palmitoleic acid, 16:0 to 16:1) (stearic acid to oleic acid, 18:0 to 18:1) as well as the content of 16:0, 16:1, 18:0, & 18:1 in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (C) The transcript level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (D & E) The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. Data were expressed as mean ± standard error of the mean. *P < 0.05, **P < 0.01, & ***P < 0.001 vs. WT group, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202415384185.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Construction of knockout (KO) & overexpression (OE) cell lines. (A) The sequencing results of KO positive clone cells; (B) The messenger RNA (mRNA) level of SREBP1 in wild type (WT) & OE Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group; (C & D) The protein level of SREBP1 in WT, OE, & KO Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-31020241539748.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - p75NTR stimulation activated SREBP1 & SREBP2 in Huh7 hepatocyte cells.Human Huh7 cells were stimulated with 10 ng/ml pro-NGF or 50 ng/ml NGF for 16 h followed by immunoblotting using antibodies to detect the presence of cleaved/activated SREBP1 & SREBP2. a SREBP1, immunoblots & b quantification. Values are mean ± SD, n = 3. **P < 0.01 & *p < 0.05 for treated vs. control cells. c, d SREBP2. Cells were treated with 10 ng/ml pro-NGF in the absence or presence of 0.5 μM PF429242 (PF), which is a selective inhibitor of the Site 1 protease (S1P). c Immunoblots & d quantification. PF decreased the amount of processed SREBP2 in these cells; however, addition of pro-NGF increased the relative level of cleaved SREBP2. Values are mean ± SD, n = 3. *p < 0.05 for treated vs. the corresponding control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31296846), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202416161836.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - p75NTR stimulation activated SREBP1 & SREBP2 in Huh7 hepatocyte cells.Human Huh7 cells were stimulated with 10 ng/ml pro-NGF or 50 ng/ml NGF for 16 h followed by immunoblotting using antibodies to detect the presence of cleaved/activated SREBP1 & SREBP2. a SREBP1, immunoblots & b quantification. Values are mean ± SD, n = 3. **P < 0.01 & *p < 0.05 for treated vs. control cells. c, d SREBP2. Cells were treated with 10 ng/ml pro-NGF in the absence or presence of 0.5 μM PF429242 (PF), which is a selective inhibitor of the Site 1 protease (S1P). c Immunoblots & d quantification. PF decreased the amount of processed SREBP2 in these cells; however, addition of pro-NGF increased the relative level of cleaved SREBP2. Values are mean ± SD, n = 3. *p < 0.05 for treated vs. the corresponding control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31296846), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202416175210.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the protein expression of Nrf2, ACC & mTORC signalling pathways in tyloxapol‐induced mice. GEN (50, 75, 100 mg/kg) was administered to WT or Nrf2−/− mice prior 1 h to stimulation of tyloxapol (500 mg/kg) for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm of WT mice was detected by Western blot. (D & E) Protein expression of Nrf2, PPAR alpha & PPAR gamma in Nrf2−/− mice was detected by Western blot. F‐H, Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta , AMPK beta in WT & Nrf2−/− mice was detected by Western blot. I‐M, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 WT & Nrf2−/− mice was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control group; *P < .05 & **P < .01 vs Tyloxapol group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202416171460.jpg)
![Immunohistochemistry-Paraffin: FoxP3 Antibody [NB100-39002] - Mouse spleen stained with FoxP3 antibody. IHC-P image submitted by a verified customer review.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-Paraffin-NB100-39002-img0011.jpg "Immunohistochemistry-Paraffin: FoxP3 Antibody [NB100-39002] - Mouse spleen stained with FoxP3 antibody. IHC-P image submitted by a verified customer review.")
![Immunohistochemistry-Paraffin: FoxP3 Antibody [NB100-39002] - Number of Granzyme B+ and FoxP3+ cells infiltrating tumors. Representative images of IHC staining of FoxP3+ and Granzyme B+ cells in the peri-tumoral areas in two mice characterized by low FoxP3+ and high Granzyme B+ (panels 1 and 2) or high FoxP3+ and low Granzyme B+ (panels 3 and 4). Image collected and cropped by Citeab from the following publication (Inhibition of tumor growth by cancer vaccine combined with metronomic chemotherapy and anti-PD-1 in a pre-clinical setting. Oncotarget (2018) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-Paraffin-NB100-39002-img0025.jpg)
![Immunohistochemistry: FoxP3 Antibody [NB100-39002] - CCR10-expressing CD4+CD25+FOXP3+ Treg cells are enriched in the spinal cord after SCI. Double immunostaining of FOXP3 (red) and CCR10 (green) in the spinal cord sections after sham or SCI surgery. The merged images are also shown. Arrows indicate cells with positive staining and colocalization. Scale bar, 100 i1/4m. Data are mean A+- SD. Image collected and cropped by Citeab from the following publication (CCL28 promotes locomotor recovery after spinal cord injury via recruiting regulatory T cells. Aging (Albany NY) (2019) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-NB100-39002-img0027.jpg)
![Flow Cytometry: FoxP3 Antibody [NB100-39002] - An intracellular stain was performed on SK-MEL-28 cells with NB100-39002 (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, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Flow-Cytometry-NB100-39002-img0022.jpg)
![Immunohistochemistry-Paraffin: FoxP3 Antibody [NB100-39002] - Tissue section of human tonsil using 1:200 dilution of rabbit anti-FoxP3 antibody. The staining was developed with HRP-labeled anti-rabbit IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This FoxP3 antibody generated an expected and a specific nuclear staining of FOXP3 in a subset of cells which are potentially the Treg cells.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-Paraffin-NB100-39002-img0017.jpg)
![Immunohistochemistry: FoxP3 Antibody [NB100-39002] - Antibody was tested in mouse spleen using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-NB100-39002-img0014.jpg)
![Immunohistochemistry-Paraffin: FoxP3 Antibody [NB100-39002] - FFPE bovine spleen tissue. Deparaffinization and antigen retrieval was carried out with PTlink from Dako, citrate buffer pH 6. Anti-Foxp3 antibody was used at a 1:100 dilution. Secondary reagent: Envision, from Dako. Staining: DAB and hematoxylin. IHC-P image submitted by a verified customer review.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-Paraffin-NB100-39002-img0024.jpg)
![Western Blot: FoxP3 Antibody [NB100-39002] - Jurkat Tag cells were transfected with the expression vector (vector) or with the Foxp3 expression construct (Foxp3). 24 hours after transfection, cells were lysed and analyzed by Western blot with anti-Foxp3 antiserum (1:2000 dilution).](http://images.novusbio.com/fullsize/FoxP3-Antibody-Western-Blot-NB100-39002-img0018.jpg)
![Immunocytochemistry/Immunofluorescence: FoxP3 Antibody [NB100-39002] - Transfectants were stained with anti-Foxp3 antibody and HRPO-conjugated (upper panel) or Cy3-conjugated (lower panels) secondary antibody. Representative images (x100) are shown.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunocytochemistry-Immunofluorescence-NB100-39002-img0012.jpg)
![Immunohistochemistry-Paraffin: FoxP3 Antibody [NB100-39002] - Tissue section of human tonsil using 1:200 dilution of rabbit anti-FoxP3 antibody. The staining was developed with HRP-labeled anti-rabbit IgG secondary antibody and DAB reagent, and nuclei of cells were counterstained with hematoxylin. This FoxP3 antibody generated an expected and a specific nuclear staining of FOXP3 in a subset of cells which are potentially the Treg cells.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Immunohistochemistry-Paraffin-NB100-39002-img0015.jpg)
![Flow Cytometry: FoxP3 Antibody [NB100-39002] - Transfectants were permeabilized and stained with anti-Foxp3 antibody and FITC-conjugated secondary antibody. Cells were analyzed by flow cytometry. Percentage of positively stained cells are shown.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Flow-Cytometry-NB100-39002-img0013.jpg)
![Flow Cytometry: FoxP3 Antibody [NB100-39002] - An intracellular stain was performed on MCF7 cells with FoxP3 Antibody NB100-39002PE (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.](http://images.novusbio.com/fullsize/FoxP3-Antibody-Flow-Cytometry-NB100-39002-img0021.jpg)
![Dual RNAscope ISH-IHC: FoxP3 Antibody [NB100-39002] - CD8A mRNA (red) and FOXP3 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-CD8A and FoxP3 antibody at 1:400 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).](http://images.novusbio.com/fullsize/FoxP3-Antibody-Dual-RNAscope-ISH-IHC-NB100-39002-img0028.jpg)
![Dual RNAscope ISH-IHC: FoxP3 Antibody [NB100-39002] - CD4 mRNA (red) and FOXP3 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-CD4 and FOXP3 antibody at 1:200 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).](http://images.novusbio.com/fullsize/FoxP3-Antibody-Dual-RNAscope-ISH-IHC-NB100-39002-img0029.jpg)
![Immunocytochemistry/ Immunofluorescence: FoxP3 Antibody - BSA Free [NB100-39002] - CCR10-expressing CD4+CD25+FOXP3+ Treg cells are enriched in the spinal cord after SCI. (A, B) Representative flow cytometry dot plots (A) & percentage (B) of CD4+CD25+FOXP3+ cells among the CD4+ T cells in the spinal cord after sham or SCI surgery. Cells were gated on 7-AAD negative population & the numbers inside plots refer to % Treg cells (n=5). (C, D) Representative histogram of CCR10 (C) & CCR3 (D) expression in CD4+CD25+FOXP3+ cells as gated in (A). (E) CD4+CD25+FOXP3+ cells in the spinal cord from sham & SCI mice were sorted out & analyzed by Western blotting to detect the expression of CCR10 & CCR3. GAPDH was used as a loading control. (F) Double immunostaining of FOXP3 (red) & CCR10 (green) in the spinal cord sections after sham or SCI surgery. The merged images are also shown. Arrows indicate cells with positive staining & colocalization. Scale bar, 100 μm. Data are mean ± SD. The statistical analysis was performed using Student’s t-test. **, P<0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31557129), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-39002_rabbit-polyclonal-foxp3-antibody-310202415541911.jpg)
![Immunocytochemistry/ Immunofluorescence: FoxP3 Antibody - BSA Free [NB100-39002] - Effects of anaphylatoxins on transcription factor phosphorylation in ARPE-19 cells. (A–C) Protein phosphorylation of (A) CREB (Ser133); (B) FoxP3 (Ser418); & (C) FOXO1 (Ser256) was examined in ARPE-19 cells treated with C3a, C5a, or the combination of C3a/C5a at 1, 5, 10, & 15 min. Phosphorylation levels were normalized to beta -actin (relative p-protein levels), & slopes of the time course were determined. Anaphylatoxins were applied at concentrations of 300 nM (C3a) & 50 nM (C5a). Data are mean + SEM, n = 3, *p < 0.05, ***p < 0.001 (Student’s t-test). (D) Immunofluorescence staining of FoxP3. Upper panel: Lewis rat (albino) eye with experimental uveitis; lower panel: normal rat eye. Asterisks mark immune cells infiltrating the retina from the choroid through the retinal pigment epithelium (RPE) in the eye with uveitis (clinical score of 2, histological score of 1). Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fimmu.2017.00703/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-39002_rabbit-polyclonal-foxp3-antibody-31020241554547.jpg)
![Simple Western: SREBP1 Antibody [NB100-2215] - Image shows a specific band for SREBP1 in 1 mg/mL of HeLa cell lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/SREBP1-Antibody-Simple-Western-NB100-2215-img0007.jpg "Simple Western: SREBP1 Antibody [NB100-2215] - Image shows a specific band for SREBP1 in 1 mg/mL of HeLa cell lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: SREBP1 Antibody [NB100-2215] - CDC2 associates with SPDY at ERES. (A-C) 0 h GV stage oocyte labeled for CDC2 (A, green), DNA (A, blue), and SPDY (B, red). Both CDC2 and SPDY localize to the same cortical domain (C). Note that the center of this oocyte is dented (the area that contains the arrow) causing the structure to appear in the middle of the oocyte, whereas it is located in the cortex. Images are Z-projections of 2 (A-C); scale bars represent 20 um in C and 5 um in C'. Arrows indicate the region of the oocyte that is shown enlarged in the insets (B'-C'). Arrowheads denote the position of the GV. Image collected and cropped by CiteAb from the following publication (//bmcdevbiol.biomedcentral.com/articles/10.1186/1471-213X-9-8) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SREBP1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2215-img0011.jpg)
![Western Blot: SREBP1 Antibody [NB100-2215] - MiR-181a overexpression impairs and miR-181a inhibition improves glucose and lipid homeostasis in HepG2 cellsHepG2 cells were divided into 4 groups as follows: a control group, mimics group (HepG2 cells transfected with 10 nM mimics), NEFA group (treated with 1. 2 mM NEFA), and miR-181a + NEFA group (transfected with 50 nM miR-181a inhibitors and then treated with 1. 2 mM NEFA). It was followed with or without 100 nM insulin. Immunoblot analysis (left) and quantification (right) of SREBP-1c and PPARI+- in HepG2 cells. Image collected and cropped by Citeab from the following publication (Upregulation of miR-181a impairs hepatic glucose and lipid homeostasis. Oncotarget (2017)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SREBP1-Antibody-Western-Blot-NB100-2215-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: SREBP1 Antibody [NB100-2215] - SREBP1 antibody was tested in HeLa cells with DyLight488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Nuclear and punctate vesicle staining was observed.](http://images.novusbio.com/fullsize/SREBP1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2215-img0006.jpg)
![Immunohistochemistry-Paraffin: SREBP1 Antibody [NB100-2215] - nalysis of FFPE tissue section of mouse liver with SREBP1 antibody at 1:200. The antibody generated an expected cytoplasmic-nuclear immunostaining of SREBP1 protein in the hepatocytes.](http://images.novusbio.com/fullsize/SREBP1-Antibody-Immunohistochemistry-Paraffin-NB100-2215-img0008.jpg)
![Western Blot: SREBP1 Antibody [NB100-2215] - Detection of SREBP1. Lane 1: human liver. Lane 2: mouse liver.](http://images.novusbio.com/fullsize/SREBP1-Antibody-Western-Blot-NB100-2215-img0004.jpg)
![Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression impairs & miR-181a inhibition improves glucose & lipid homeostasis in HepG2 cellsHepG2 cells were divided into 4 groups as follows: a control group, mimics group (HepG2 cells transfected with 10 nM mimics), NEFA group (treated with 1.2 mM NEFA), & miR-181a + NEFA group (transfected with 50 nM miR-181a inhibitors & then treated with 1.2 mM NEFA). B was followed with or without 100 nM insulin. (A) Immunoblot analysis (top) & quantification (bottom) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in HepG2 cells. (B) Immunoblotting analysis (top) & quantification (bottom) of insulin-stimulated phosphorylation of AKT in HepG2 cells. (C) Glucose concentration in medium. (D) The glycogen content in HepG2 cells. (E) The mRNA expression levels of G6Pase & PEPCK. (F) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha in HepG2 cells. (G) TG content in HepG2 cells. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2215_rabbit-polyclonal-srebp1-antibody-31020241682194.jpg)
![Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - Effect of restoration of macrophage A2bAR on liver.Liver was collected from WT, A2bAR KO, & CD68-Tg mice after 16 weeks of HFD as described in the methods. Relative mRNA expression was determined using the delta delta CT method with normalization to 18s rRNA. A. mRNA expression of TNF-alpha in liver. A2bAR KO (n = 5) vs WT (n = 7) p-value = 0.0271; A2bAR KO vs CD68-Tg (n = 6) p-value = 0.0210. B. mRNA expression of IL-6 in liver. A2bAR KO (n = 8) vs WT (n = 7) p-value = 0.0159; A2bAR KO vs CD68-Tg (n = 8) p-value = 0.0080. C. mRNA expression of IRS-2 in liver. CD68-Tg (n = 7) vs A2bAR KO (n = 8) p-value = 0.0300. D. Western blot analysis of liver; one representative (of 3 sets) WT, CD68-Tg & A2bAR KO group shown at 15 minutes post-insulin injection, following 16 weeks of HFD. Levels of mature SREBP-1 (68 kDa), & IRS-2 (185 kDa), were probed by Western blot analysis, using beta -actin (43 kDa) as loading control. Quantification of Western Blot results was performed with Image J software (//rsb.info.nih.gov/ij/) with normalization to beta -actin. WT to A2bAR KO: IRS-2 p-value = 0.0092, SREBP-1 p-value = 0.0154; CD68-Tg to A2bAR KO: IRS-2 p-value = 0.0247, SREBP-1 p-value = 0.0170. Data are averages ± SD. *Student two-tail t-test assuming equal variance was found significant only when p-value <0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24892847), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2215_rabbit-polyclonal-srebp1-antibody-31020241682175.jpg)
![Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression or SIRT1 knockdown impairs glucose & lipid metabolism in vivo(Aa & Ab) Immunoblotting analysis (left) & quantification (right) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in the liver of mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (B) Glucose tolerance test of mice injected with Ago-181a (n = 7) or Ago-NC (n = 7) or Ad-shRNA NC (n = 6) or Ad-shRNA SIRT1 (n = 6). (C) Insulin tolerance test of mice injected with Ago-181a (n = 7) or Ago-NC (n = 7) or Ad-shRNA NC (n = 6) or Ad-shRNA SIRT1 (n = 6). (D) Representative images of PAS staining (original magnification × 20) of liver sections from mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (Ea & Eb) Immunoblotting analysis (top) & quantification (bottom) of insulin-stimulated phosphorylation of IR, AKT & GSK3 beta in liver of mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (F) Representative images of H&E staining (left, original magnification × 20) & Oil-red staining (right, original magnification × 20) of liver sections from mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (Ga & Gb) Immunoblotting analysis (top) & quantification (bottom) of SREBP-1c & PPAR alpha in the liver of mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2215_rabbit-polyclonal-srebp1-antibody-31020241553209.jpg)
![Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression impairs & miR-181a inhibition improves glucose & lipid metabolism in vitro(A, B, C, D & E) Hepatocytes were transfected with 10 nM miR-181a mimics or negative controls in the absence or presence of 100 nM insulin. (A) Immunoblot analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, Akt & GSK3 beta in hepatocytes. (B) The mRNA expression levels of G6Pase & PEPCK in hepatocytes. (C) Glucose concentration in medium. (D) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha expression in hepatocytes. (E) TG content in hepatocytes. (F, G, H, I & J) Hepatocytes were transfected with 50 nM miR-181a inhibitors or negative controls in the absence or presence of 100 nM insulin. (F) Immunoblot analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, Akt & GSK3 beta in hepatocytes. (G) The expression levels of G6Pase & PEPCK in hepatocytes. (H) Glucose concentration in medium. (I) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha expression in hepatocytes. (J) TG content in hepatocytes. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2215_rabbit-polyclonal-srebp1-antibody-310202415535169.jpg)
![Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - Effect of restoration of macrophage A2bAR on adipose tissue.Visceral (epididymal) adipose tissue was collected from WT, A2bAR KO, & CD68-Tg mice after 16 weeks of HFD as described in the methods. A-C,E. Relative mRNA expression was determined using the delta delta CT method with normalization to 18s rRNA. A. mRNA expression of TNF-alpha in visceral fat. A2bAR KO (n = 7) vs CD68-Tg (n = 9) p-value = 0.0345. B. mRNA expression of IL-6 in visceral fat. A2bAR KO (n = 7) vs WT (n = 7) p-value = 0.0073; A2bAR KO vs CD68-Tg (n = 7) p-value = 0.0141. C. mRNA expression of MCP1 in visceral fat. A2bAR KO (n = 7) vs CD68-Tg (n = 9) p-value = 0.0232. D. Visceral adipose tissue from WT, A2bAR KO, & CD68-Tg mice after 16 weeks of HFD was fixed in 4% paraformaldehyde & paraffin-embedded. Sections immunostained with the macrophage marker F4/80. Representative sections for each genotype at a magnification of 200x & 400x. Arrows point to crown-like structures. E. mRNA expression of IRS-2 in visceral fat. CD68-Tg (n = 8) vs A2bAR KO (n = 8) p-value = 0.0115, WT (n = 6) vs A2bAR KO p-value = 0.0358. F. Western blot analysis of visceral fat; one representative (of 3 sets) WT, CD68-Tg & A2bAR KO group shown at 15 minutes post-insulin injection, following 16 weeks of HFD. WT to A2bAR KO: IRS-2 p-value = 0.0411, SREBP-1 p-value = 0.0103. CD68-Tg to A2bAR KO: IRS-2 p-value = 0.0305, SREBP-1 p-value = 0.0459. Data are averages ± SD. *Student two-tail t-test assuming equal variance was found significant only when p-value <0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24892847), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2215_rabbit-polyclonal-srebp1-antibody-31020241682189.jpg)
![Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - SIRT1 knockdown impairs & SIRT1 overexpression improves glucose & lipid metabolism in hepatocytes(A) Immunoblot analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, Akt & GSK3 beta protein levels in hepatocytes. Hepatocytes were transfected with SIRT1 siRNA with or without 100 nM insulin. (B) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha protein levels in hepatocytes. Hepatocytes were transfected with SIRT1 siRNA. (C) Immunoblot analysis (left) & quantification (right) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in hepatocytes. Hepatocytes were infected with Ad-SIRT1. (D) Immunoblotting analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, AKT & GSK3 beta in hepatocytes. Hepatocytes were treated with 1.2 mM NEFA or 1.2 mM NEFA & Ad-SIRT1 with or without 100 nM insulin. (E, F & G) Hepatocytes were treated with 1.2 mM NEFA or 1.2 mM NEFA & Ad-SIRT1. (E) Glucose concentration in medium. (F) Immunoblot analysis (top) & quantification (bottom) of SREBP-1c & PPAR alpha in hepatocytes. (G) TG contents in hepatocytes. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2215_rabbit-polyclonal-srebp1-antibody-310202415541953.jpg)