| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-135SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-27409 | |||
| BSA Free | NB100-56704SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-92693SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-77686SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-241SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-270SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-55376SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB500-176SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB120-6106SS | |||
| Azide and BSA Free | NBP2-80778 | |||
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0025.jpg "Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.")
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP in rat tissue samples. Image courtsey of product review by Daniel Pirici.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0011.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43/TARDBP and is increased in mutant TDP-43 transgenic mouse spinal cords. Co-immunoprecipitation of wildtype and mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations were performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype and Q331K cell lysates. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0028.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on HeLa cell. Antibody concentration 10 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunocytochemistry-Immunofluorescence-H00023435-M01-img0019.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma. [antibody concentration 3 ug/ml]](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0013.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP expression in transfected 293T cell line by TARDBP monoclonal antibody (M01), clone 2E2-D3.Lane 1: TARDBP transfected lysate(44.7 KDa).Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0026.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma tissue Antibody concentration 3 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0021.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP over-expressed 293 cell line, cotransfected with TARDBP Validated Chimera RNAi ( Cat # H00023435-R01V ) (Lane 2) or non-transfected control (Lane 1). Blot probed with TARDBP monoclonal antibody (M01), clone 2E2-D3 (Cat # H00023435-M01 ). GAPDH ( 36.1 kDa ) used as specificity and loading control.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0023.jpg)
![ELISA: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Detection limit for recombinant GST tagged TARDBP is 0.3 ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-ELISA-H00023435-M01-img0027.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43 & is increased in mutant TDP-43 transgenic mouse spinal cords.(A) Co-immunoprecipitation of wildtype & mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype & Q331K cell lysates. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415284521.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - CLIP shows that TDP-43 directly interacts with translational target mRNAs. (A) Schematic diagram of the CLIP experiment. (B) Immunoblot showing specific IP of TDP-43 from MN1 cells under CLIP conditions. A TDP-43 band is specifically observed in the input & TDP-43 IP lanes from both untreated & UV-treated cells, but not in the IgG or anti-RBP X control lanes. RBP X is an IP of a different RNA-binding protein, which serves as an additional specificity control here. (C and D) Plots showing percentage of input mRNA in the TDP-43 IP for the mRNAs indicated in three separate CLIP assays from MN1 cells. Performing CLIP from UV-treated cells leads to significant recovery & enrichment relative to Gapdh for all mRNAs examined (C). In the absence of UV treatment, much less mRNA is recovered & no significant enrichment relative to Gapdh mRNA is observed. Note that the Y-axis scale in D is 1000× smaller than in C, indicating strong crosslinking dependence of mRNA co-immunoprecipitation (n = 3, s.e.m. error bars, P-values indicated in the plot, unpaired two-tailed t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30357366), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415483647.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - SINE compounds partially rescue motor deficits in an animal model of ALS/FTD. (a) Schematic timeline for in vivo experiments. (b) Western blot demonstrating the expression of human TDP43 within the brains of AAV9-injected animals, which we have previously shown is largely restricted to neuronal cell types (Jackson et al.59). Full-length blots appear in Fig. S1. (c) The hang test measures the time it takes for animals to fall from grid-like scaffold when it is lifted & tilted. A single representative animal administered AAV9-TDP43 is shown; note the inability of the hind limbs to clasp the wire mesh. (d) TDP43 expression impaired motor performance on the hang test at 3 weeks, an effect that could be mitigated by 7.5 mg kg-1 KPT-350. (e) Rotarod testing at 4 weeks of age showed prominent deficits associated with TDP43 expression that were resistant to treatment with SINE compounds. n, number of animals per condition. ns, not significant, mean ± s.e.m. *p < 0.05, **p < 0.01, ***p < 0.001, one-way ANOVA with Bonferroni correction. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-22858-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415482260.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.](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)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of human IKK alpha in tumors of the three groups B (C-IKK alpha), E (Control), H (N-IKK alpha). Specific staining of human IKK alpha-using the NB100-56704 antibody. Scale bar: 70um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0018.jpg "Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of human IKK alpha in tumors of the three groups B (C-IKK alpha), E (Control), H (N-IKK alpha). Specific staining of human IKK alpha-using the NB100-56704 antibody. Scale bar: 70um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.")
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Western blot showing the increased expression of IKK-alpha in transgenic mice. Image collected and cropped by CiteAb from the following publication (oncotarget.com/fulltext/8792), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0021.jpg)
![Flow Cytometry: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - An intracellular stain was performed on Hek293 cells with IKK alpha Antibody (14A231) NB100-56704 (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 Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Flow-Cytometry-NB100-56704-img0017.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Total protein from various Human, Mouse and Rat cell lines were 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 1.0 ug/mL anti-IKK-alpha in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). An antibody dilution of 1:10 was used. Image objective 40X.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0008.jpg)
![Immunohistochemistry: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - B-I. Immunohistochemistry showing the expression of the transgenic protein in N-IKKa and C-IKKa tumors. Staining with NB100-56704 antibody is shown. (B, C) Representative images showing the expression of transgenic IKKa in tumors and adjacent skin of N-IKKa/TgAC mice (B), and C-IKKa/TgAC animals (C). (D, E) Detail showing the nuclear (D) or cytoplasmic (E) localization of the transgenic IKKa in tumors. (F, G) Similar levels of expression of the transgenic IKKa in different N-IKKa tumors. By contrast variable levels of expression of the transgene are observed between different C-IKKa tumors (H, I). t: tumor; s: non-tumoral skin. Scale bar: (B, C) 100um; (D, E) 80 um; (F-I) 200 um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-NB100-56704-img0022.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Analysis of IKK alpha in Daudi cell lysate using IKK alpha antibody at 1 ug/mL.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - A431 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-IKK alpha Antibody (14A231) at 2 ug/mL overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-IKK alpha Antibody (14A231) at 2 ug/mL overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0015.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of a FFPE tissue section of human kidney using 1:200 dilution of IKK alpha clone 14A231 antibody. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0016.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha and N-IKK alpha mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is shown. Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) and in cells surrounding the sebaceous glands (sb). Scale bar: 60um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0020.jpg)
![Simple Western: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Image shows a specific band for IKK alpha in 0.5 mg/mL of Daudi (left) and U937 (right) lysate. This exeriment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Simple-Western-NB100-56704-img0009.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - NEMO-Ub binding is essential for TNF alpha signaling, but not for IL-1 beta signaling.(a) Schematic illustration of NEMO deletions or point mutations. (b,c) Effects of NEMO C-terminal deletion mutants on TNF alpha & IL-1 beta signaling. NEMO−/Y MEFs were reconstituted with mock, NEMO WT or different C-terminal deletion constructs & stimulated with TNF alpha (b) or IL-1 beta (c). Effects on NF-kappa B signaling were investigated by determining I kappa B alpha phosphorylation & degradation in Western Blots as well as NF-kappa B-DNA binding by EMSA. (d,e) Effects of NEMO D311N on TNF alpha & IL-1 beta signaling. NEMO−/Y MEFs were reconstituted with mock, NEMO WT or NEMO D311N point mutant & stimulated with TNF alpha (d) or IL-1 beta (e). Analysis on NF-kappa B signaling were performed as in (b,c). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26740240), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-310202415392529.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha & N-IKK alpha miceA. Recombinant DNA constructs employed to generate both transgenic mice lines. For C-IKK alpha mice generation, the nuclear localization signal (NLS) was removed from the sequence of the human IKK alpha cDNA employed. In the construct used for generation of the N-IKK alpha mice an extra NLS signal was added. WT IKK alpha ; wild type IKK alpha . B. Western blot of total protein extracts showing IKK alpha expression in back skin of Control & C-and N-IKK alpha mice. Actin was used as a loading control. C. Representative example of the K5 staining in back skin section of Control mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is showed; similar results were obtained with the H00001147-M04 IKK alpha antibody (not shown). Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) & in cells surrounding the sebaceous glands (sb). F. Back skin section of Control mice. The NB100-56704 antibody used does not recognize the endogenous IKK alpha in immunohistochemical assays. G. Endogenous IKK alpha expression in control mice using the IKK alpha (sc-7182) antibody. Scale bar: (C) 70 μm; (D-G) 60 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-310202415523920.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha & N-IKK alpha miceA. Recombinant DNA constructs employed to generate both transgenic mice lines. For C-IKK alpha mice generation, the nuclear localization signal (NLS) was removed from the sequence of the human IKK alpha cDNA employed. In the construct used for generation of the N-IKK alpha mice an extra NLS signal was added. WT IKK alpha ; wild type IKK alpha . B. Western blot of total protein extracts showing IKK alpha expression in back skin of Control & C-and N-IKK alpha mice. Actin was used as a loading control. C. Representative example of the K5 staining in back skin section of Control mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is showed; similar results were obtained with the H00001147-M04 IKK alpha antibody (not shown). Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) & in cells surrounding the sebaceous glands (sb). F. Back skin section of Control mice. The NB100-56704 antibody used does not recognize the endogenous IKK alpha in immunohistochemical assays. G. Endogenous IKK alpha expression in control mice using the IKK alpha (sc-7182) antibody. Scale bar: (C) 70 μm; (D-G) 60 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-3102024168399.jpg)
![Analysis of whole brain tissue lysates using mouse mAb to FOX3/NeuN NBP1-92693, dilution 1:1,000 in green: [1] protein standard (red), [2] adult rat brain, [3] embryonic E20 rat brain, [4] adult mouse brain. Note the strong twin bands corresponding to the two alternate transcripts of FOX3/NeuN protein with apparent SDS-PAGE molecular weights of 46 and 48kDa. As with other FOX3/NeuN antibodies, an additional band at ~70kDa is revealed in some lysates.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-1B7-Western-Blot-NBP1-92693-img0020.jpg)
![Immunocytochemistry/ Immunofluorescence: RBFOX3/NeuN Antibody (1B7) [NBP1-92693] - NF kappa B localizes to both neuronal & glial nuclei in superior colliculus. Representative confocal images of NF kappa B in the superior colliculus (SC) of vehicle- & HE3286-treated rats with all nuclei indicated (DAPI). Sections were also labeled for astrocytes (A, GFAP), microglia (B, Iba1), or neurons using antibodies against either NeuN (C) or phosphorylated neurofilament heavy (pNFH; D). Representative nuclei from each cell class demonstrated NF kappa B localization (arrows). Insets (solid white, B) show region contained within dashed box with red channel removed to better visualize nuclear localization of NF kappa B. Scale: 10 μm. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnins.2017.00045/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-92693_mouse-monoclonal-rbfox3-neun-antibody-1b7-310202415382419.jpg)
![Immunohistochemistry-Paraffin: RBFOX3/NeuN Antibody [NBP1-77686] - IHC analysis of formalin fixed paraffin embedded tissue section from hippocampus of mouse brain with NeuN antibody at 1:200 dilution. The antibody generated a strong nuclear with weak cytoplasmic staining in NeuN reactive cells.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Immunohistochemistry-Paraffin-NBP1-77686-img0007.jpg "Immunohistochemistry-Paraffin: RBFOX3/NeuN Antibody [NBP1-77686] - IHC analysis of formalin fixed paraffin embedded tissue section from hippocampus of mouse brain with NeuN antibody at 1:200 dilution. The antibody generated a strong nuclear with weak cytoplasmic staining in NeuN reactive cells.")
![Immunohistochemistry-Paraffin: RBFOX3/NeuN Antibody [NBP1-77686] - JAK3 colocalized with neurons labeled with NeuN. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fneur.2017.00363/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Immunohistochemistry-Paraffin-NBP1-77686-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: RBFOX3/NeuN Antibody [NBP1-77686] - Neuro2a 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 anti-RBFOX3/NeuN Antibody NBP1-77686 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/RBFOX3-NeuN-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-77686-img0013.jpg)
![Western Blot: RBFOX3/NeuN Antibody [NBP1-77686] - Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Western-Blot-NBP1-77686-img0012.jpg)
![Flow Cytometry: RBFOX3/NeuN Antibody [NBP1-77686] - An intracellular stain was performed on Hek293 cells with NBP1-77686AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Flow-Cytometry-NBP1-77686-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: RBFOX3/NeuN Antibody [NBP1-77686] - NeuN antibody was tested in U2OS cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-77686-img0005.jpg)
![Immunohistochemistry: RBFOX3/NeuN Antibody [NBP1-77686] - Analysis of NeuN in mouse brain using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Immunohistochemistry-NBP1-77686-img0008.jpg)
![Flow Cytometry: RBFOX3/NeuN Antibody [NBP1-77686] - An intracellular stain was performed on U2OS cells with RBFOX3/NeuN Antibody NBP1-77686AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/RBFOX3-NeuN-Antibody-Flow-Cytometry-NBP1-77686-img0009.jpg)
![Immunocytochemistry/ Immunofluorescence: RBFOX3/NeuN Antibody - BSA Free [NBP1-77686] - Double immunofluorescence indicates that NF-kappa B & CCL5 were co-localized with microglia, astrocytes, & neurons in the ipsilateral L4–5 spinal cord on day 7 after CCI.NF-kappa B (green) colocalizes with Iba-1, GFAP, & NeuN (red) in laminae II–III of the superficial dorsal horn (A). CCL5 (red) co-localizes with Iba-1, GFAP, & NeuN (green) in the medial superficial dorsal horn (laminae II–III) (B). NF-kappa B (green) co-localizes with CCL5 (red) in laminae II–IV of the superficial dorsal horn following CCI on day 7 in the sham & CCI groups in the ipsilateral L4–5 spinal cord (C). Two single stained images (yellow) were merged. Scale = 100 μm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0115120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77686_rabbit-polyclonal-rbfox3-neun-antibody-31020241538241.jpg)
![Immunocytochemistry/ Immunofluorescence: RBFOX3/NeuN Antibody - BSA Free [NBP1-77686] - (A) Representative Western blots depicting phosphorylated JAK3 (pJAK3), total JAK3, & corresponding beta -actin levels in the ipsilateral (CXI) versus the contralateral (CXC) cortex at 24 h in sham & mice subjected to permanent middle cerebral artery occlusion (pMCAO). (B,C) Quantified pJAK3 & JAK3 values normalized to beta -actin in the cortex of sham & mice subjected to stroke. Both pJAK3 & JAK3 are significantly increased in the ipsilateral cortex of stroked animals (*P < 0.05 & **P < 0.01 with respect to sham ipsilateral/contralateral & stroke contralateral; sham, n = 5; stroke, n = 13). Data were analyzed using a two-way ANOVA (ipsilateral/contralateral or sham/stroke) with Bonferroni post-test. (D) Diagram showing peri-infarct brain region from which images were taken (n = 3). Scale bar is 10 µm, & magnification is 60×. (E) JAK3 colocalized with microglia/macrophages labeled with Iba-1. (F) JAK3 colocalized with neurons labeled with NeuN. (G) JAK3 colocalized with endothelial cells labeled with CD31. (H) JAK3 is not colocalized with astrocytes labeled with GFAP. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28790974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77686_rabbit-polyclonal-rbfox3-neun-antibody-310202416175267.jpg)
![Western Blot: 4EBP1 Antibody [NB200-157] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and 4EBP1 knockout (KO) HeLa cell line. PVDF membrane was probed with 0.5 ug/ml of Rabbit Anti-Human 4EBP1 Polyclonal Antibody (Catalog # NB200-157) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for 4EBP1 at approximately 17-20 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/4EBP1-Antibody-Knockout-Validated-NB200-157-img0011.jpg "<b>Genetic Strategies Validation. </b>Western Blot: 4EBP1 Antibody [NB200-157] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and 4EBP1 knockout (KO) HeLa cell line. PVDF membrane was probed with 0.5 ug/ml of Rabbit Anti-Human 4EBP1 Polyclonal Antibody (Catalog # NB200-157) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for 4EBP1 at approximately 17-20 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.")
![<b>Genetic Strategies Validation. </b>Western Blot: 4EBP1 Antibody [NB200-157] - Whole cell lysate (100 ug) from RINm5F insulinoma exposed to high or low concentration of leucine. Antibody used at 0.25 ug/ml.](http://images.novusbio.com/fullsize/4EBP1-Antibody-Western-Blot-NB200-157-img0009.jpg)
![Immunohistochemistry: 4EBP1 Antibody [NB200-157] - Sample: FFPE section of human breast carcinoma. Antibody: Affinity purified rabbit anti-4EBP1 used at a dilution of 1:20,000 ( 0.05ug/ml). Detection: DAB staining using Immunohistochemistry Accessory Kit.](http://images.novusbio.com/fullsize/4EBP1-Antibody-Immunohistochemistry-NB200-157-img0010.jpg)
![Western Blot: Rabbit Polyclonal 4EBP1 Antibody [NB200-157] - Whole cell lysates from MDA-MB-231, SUM159 and MCF-7 cells were loaded with 50 ug/lane. 10% SDS-PAGE. 4EBP1 Antibody (NB200-157) was used for primary antibody: 1:2000, 4C, overnight. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb200-157_rabbit-polyclonal-4ebp1-antibody-western-blot-311202415623..png)
![Immunocytochemistry/Immunofluorescence: Nucleolin Antibody [NB600-241] - Analysis of Nucleolin MCF-7 breast cancer cells. Image courtsey of product review by Lacey Litchfield.](http://images.novusbio.com/fullsize/Nucleolin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-241-img0008.jpg "Immunocytochemistry/Immunofluorescence: Nucleolin Antibody [NB600-241] - Analysis of Nucleolin MCF-7 breast cancer cells. Image courtsey of product review by Lacey Litchfield.")
![Simple Western: Nucleolin Antibody [NB600-241] - Image shows a specific band for Nucleolin 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/Nucleolin-Antibody-Simple-Western-NB600-241-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: Nucleolin Antibody [NB600-241] - Endogenous nuclear nucleolin-COUP-TFII interaction in MCF-7 and T47D cells.NE (200A ug protein) from MCF-7 cells. Immunofluorescent staining of endogenous COUP-TFII (green) and nucleolin (red) in the nuclei (Hoechst, blue) of MCF-7 cells. Merged images are shown at the right. Bar is 10A um. Image collected and cropped by Citeab from the following publication (Identification and characterization of nucleolin as a COUP-TFII coactivator of retinoic acid receptor transcription in breast cancer cells. PLoS One (2012) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Nucleolin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-241-img0012.jpg)
![Western Blot: Nucleolin Antibody [NB600-241] - Detection of nucleolin in crude PD31 nuclear extracts.](http://images.novusbio.com/fullsize/Nucleolin-Antibody-Western-Blot-NB600-241-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Nucleolin Antibody [NB600-241] - Human prostate epithelial cells stained with anti-nucleolin (red), CFSE (green) retaining cell has increased nucleolin in nucleolus. DAPI (blue). Image from verified customer review.](http://images.novusbio.com/fullsize/Nucleolin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-241-img0011.jpg)
![Immunohistochemistry: Nucleolin Antibody [NB600-241] - Detection of Nucleolin in human tonsil germinal center.](http://images.novusbio.com/fullsize/Nucleolin-Antibody-Immunohistochemistry-NB600-241-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: Nucleolin Antibody [NB600-241] - In-situ immunofluorescent staining of PD31 murine pre-B cells.](http://images.novusbio.com/fullsize/Nucleolin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-241-img0007.jpg)
![Western Blot: Nucleolin Antibody [NB600-241] - HT-LKO cells recapitulate the hallmarks of lamin A/C deficiency.(a) Quantitative PCR shows a >6-fold reduction (expressed as log2 fold change of ddCt value) of LMNA transcripts in different LKO colonies as compared to HT-WT clones; (b) Quantitative immunofluorescence shows a dramatic reduction of A-type lamin levels in HT-LKO colonies, approximating background levels (dotted white line); (c) Western blot for lamin A/C reveals the absence of both proteins in HT-LKO cells; (d) Immunostaining & nuclear counterstaining of HT-LKO cells reveals their aberrant nuclear morphology, virtual absence of lamin A (green) & local depletion of lamin B (red) (arrowheads) as opposed to HT-WT cells; (e) Time-lapse recordings after H2B-GFP transfection illustrate increased nuclear plasticity of HT-LKO vs. HT-WT cells, as evidenced by their larger projected area (Σ Area) & contour changes (Σ Outline) across time; (f) HT-LKO nuclei have a lower average nuclear circularity (dotted white line indicates a circularity of 0.85) & higher nuclear circularity fluctuations (average + 95% confidence interval) than HT-WT cells; The Y-axis has been cropped for clarity; (g) This translates into a significantly larger coefficient of variation (CoV) for the circularity across time (p < 0.001). (h) Nuclear ruptures occur more frequently in HT-LKO cells than in HT-WT cells (p < 0.001); (i) Representative montages of the NLS channel of a C4 HT-WT & L2 HT-LKO cell, with corresponding NLS/H2B ratio measurements (grey-coded bar plots). The moments of rupture events are indicated as red dots. Bar graphs reflect mean ± standard error (n = number of tracks). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27461848), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-241_rabbit-polyclonal-nucleolin-antibody-310202416165620.jpg)
![Simple Western: Park7/DJ-1 Antibody [NB300-270] - Simple Western lane view shows a specific band for Park7 (DJ-1) in 0.05 mg/ml of Human Brain lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Simple-Western-NB300-270-img0009.jpg "Simple Western: Park7/DJ-1 Antibody [NB300-270] - Simple Western lane view shows a specific band for Park7 (DJ-1) in 0.05 mg/ml of Human Brain lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - Lysates of the human RPE cell lines ARPE-19 (lane 1) and D407 (lane 2), the mouse RPE cell line B6-RPE07 (lane 3), mouse primary RPE (lane 4) and mouse brain lysates (lane 5) were harvested and analyzed by immunoblot assay with DJ-1 antibody. The DJ-1 signal varied in intensity in each RPE cell culture. Each lane contained 20 ug of protein. Protein loads were confirmed in replicate blots probed with GAPDH. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067983), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Western-Blot-NB300-270-img0014.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Park7/DJ-1 Antibody [NB300-270] - Representative confocal micrographs of ARPE-19 monolayers plated on Transwells(R) and labeled with antibodies to DJ-1 (G,J) and COX IV (H,K). Under baseline conditions, there is very little colocalization between DJ-1 and COX IV, as observed in overlaid images (I); DJ-1 is mostly distributed through the cytoplasm (arrows). Upon oxidative stress induced by incubation with 400 uM H2O2 for 1 hr, DJ-1 staining is increased (arrowheads) in ARPE-19 (J) cultures. In cultures treated with H2O2 some DJ-1 re-distributed to mitochondria (arrowheads) and displayed significant colocalization with COX IV in overlaid images (L). Scale bar = 10 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067983), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-270-img0015.jpg)
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - ARPE-19 and D407 monolayers were treated with increasing concentrations (0 to 800 uM) of H2O2 for 18 hrs (B), harvested, and analyzed by immunoblot assay with DJ-1 antibody (upper panel). Each lane contained 20 ug of protein. Protein loadings were confirmed in replicate blots probed with GAPDH (lower panel). A representative Western is shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067983), licensed under a CC-BY license](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Western-Blot-NB300-270-img0013.jpg)
![Immunohistochemistry-Paraffin: Park7/DJ-1 Antibody [NB300-270] - Park7(DJ-1) detected in paraffin embedded human cortex.](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Immunohistochemistry-Paraffin-NB300-270-img0007.jpg)
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - Human HEK293 cells and mouse brain lysates.](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Western-Blot-NB300-270-img0005.jpg)
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - Cells were transfected with the pCMV6-ENTRY control (lane 1) or pCMV6-ENTRY PARK7 cDNA (lane 2) for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-Park7(DJ-1).](http://images.novusbio.com/fullsize/Park7-DJ-1-Antibody-Western-Blot-NB300-270-img0008.jpg)
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - Presence of oxDJ-1 in RPE cells subjected to oxidative stress.ARPE-19 monolayers were treated with increasing concentrations (0 to 800 µM) of H2O2 for 1 hr (A) & 18 hs (B), harvested, & analyzed by immunoblot assay with oxDJ-1 antibody (upper panel). Protein loadings were confirmed in replicate blots probed with GAPDH (lower panel). Each lane contained 20 µg of protein. A dose response is observed when cells are exposed to increasing concentrations of H2O2 for 1 h (A, lanes 1 to 6) & 18 hrs (B, lanes 7 to 12). Confocal immunofluorescence staining of baseline ARPE-19 cultures (C) fixed before extraction with Triton X-100 & labeling with oxDJ-1 antibodies revealed absence of oxDJ-1. However, oxDJ-1 is observed in the cytoplasm (arrows) & perinuclear area (arrowheads) of RPE cells exposure to 400 µM H2O2 for 1 h (D) & 18 hrs (E). Cell nuclei were labeled with TO-PRO-3. Scale bar = 20 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23844142), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-270_rabbit-polyclonal-park7-dj-1-antibody-31020241621815.jpg)
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - Presence of oxDJ-1 in RPE cells subjected to oxidative stress.ARPE-19 monolayers were treated with increasing concentrations (0 to 800 µM) of H2O2 for 1 hr (A) & 18 hs (B), harvested, & analyzed by immunoblot assay with oxDJ-1 antibody (upper panel). Protein loadings were confirmed in replicate blots probed with GAPDH (lower panel). Each lane contained 20 µg of protein. A dose response is observed when cells are exposed to increasing concentrations of H2O2 for 1 h (A, lanes 1 to 6) & 18 hrs (B, lanes 7 to 12). Confocal immunofluorescence staining of baseline ARPE-19 cultures (C) fixed before extraction with Triton X-100 & labeling with oxDJ-1 antibodies revealed absence of oxDJ-1. However, oxDJ-1 is observed in the cytoplasm (arrows) & perinuclear area (arrowheads) of RPE cells exposure to 400 µM H2O2 for 1 h (D) & 18 hrs (E). Cell nuclei were labeled with TO-PRO-3. Scale bar = 20 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23844142), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-270_rabbit-polyclonal-park7-dj-1-antibody-3102024162185.jpg)
![Western Blot: Park7/DJ-1 Antibody [NB300-270] - Presence of oxDJ-1 in RPE cells subjected to oxidative stress.ARPE-19 monolayers were treated with increasing concentrations (0 to 800 µM) of H2O2 for 1 hr (A) & 18 hs (B), harvested, & analyzed by immunoblot assay with oxDJ-1 antibody (upper panel). Protein loadings were confirmed in replicate blots probed with GAPDH (lower panel). Each lane contained 20 µg of protein. A dose response is observed when cells are exposed to increasing concentrations of H2O2 for 1 h (A, lanes 1 to 6) & 18 hrs (B, lanes 7 to 12). Confocal immunofluorescence staining of baseline ARPE-19 cultures (C) fixed before extraction with Triton X-100 & labeling with oxDJ-1 antibodies revealed absence of oxDJ-1. However, oxDJ-1 is observed in the cytoplasm (arrows) & perinuclear area (arrowheads) of RPE cells exposure to 400 µM H2O2 for 1 h (D) & 18 hrs (E). Cell nuclei were labeled with TO-PRO-3. Scale bar = 20 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23844142), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-270_rabbit-polyclonal-park7-dj-1-antibody-310202416212344.jpg)
![Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - Total protein from HeLa, MCF7 and mouse brain 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 1.0 ug/ml anti-TARDBP in 1% block buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Western-Blot-NB110-55376-img0012.jpg "Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - Total protein from HeLa, MCF7 and mouse brain 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 1.0 ug/ml anti-TARDBP in 1% block buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.")
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - HeLa 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 TDP-43/TARDBP Antibody conjugated to Alexa Fluor 488 (NB110-55376AF488) at 10 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton X-100. The cells were incubated with anti-TARDBP at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0011.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody [NB110-55376] - Analysis of FFPE human placenta using TDP-43 antibody at 1:250 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Nuclear staining was observed. Staining was performed by Histowiz.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunohistochemistry-Paraffin-NB110-55376-img0010.jpg)
![Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - TARDBP antibody was tested in HeLa WCE.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Western-Blot-NB110-55376-img0004.jpg)
![Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - Cells were transfected with the pCMV6-ENTRY control or pCMV6-ENTRY TARDBP cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-TARDBP.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Western-Blot-NB110-55376-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - TARDBP antibody was tested in MCF-7 cells with DyLight 488 (Green). Nuclei and alpha-tubulin were counterstained with DAPI (Blue) and DyLight 550 (Red).](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - Analysis using the DyLight 550 conjugate of NB110-55376. Staining of Human iPS derived neurons, fixed in 4% formaldehyde solution. NB110-55376R was diluted 1:200. All antibodies were diluted in PBS/BSA 3% (w/v) ) Triton X-100 0,3 % (v/v). Images taken by an Arrayscan (Cellomics). Blue dots in TDP staining is Hoechst.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - Subcellular distribution of TDP-43 and CWC22 in control DRG sensory neurons. TDP-43 was stained diffusely in the nucleus, excluding SMN foci in sensory neurons. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//dmm.biologists.org/lookup/doi/10.1242/dmm.028225) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0013.jpg)
![Western Blot: POT1 Antibody [NB500-176] - Detection of POT1 in HeLa nuclear extracts (25 ug) using NB500-176(1:500). ECL detection 1 min.](http://images.novusbio.com/fullsize/POT1-Antibody-Western-Blot-NB500-176-img0003.jpg "Western Blot: POT1 Antibody [NB500-176] - Detection of POT1 in HeLa nuclear extracts (25 ug) using NB500-176(1:500). ECL detection 1 min.")
![<b>Biological Strategies Validation. </b>Western Blot: POT1 Antibody [NB500-176] - Immunoblotting assessment of TRF1, TRF2 and POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 and POT1 protein levels and shown was representative of three independent experiments. BGC-823-hTERT cells. Image collected and cropped by Citeab from the following publication (Bortezomib-mediated down-regulation of telomerase and disruption of telomere homeostasis contributes to apoptosis of malignant cells. Oncotarget (2015) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/POT1-Antibody-Western-Blot-NB500-176-img0004.jpg)
![Western Blot: KAP1 Antibody [NB500-158] - Whole cell lysate (50 ug) from NIH 3T3, TCMK-1, 4T1, CT26.WT, and rat C6 cells. Antibodies: Affinity purified rabbit anti-KAP-1 antibody used for WB at 1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes.](http://images.novusbio.com/fullsize/KAP1-Antibody-Western-Blot-NB500-158-img0028.jpg "Western Blot: KAP1 Antibody [NB500-158] - Whole cell lysate (50 ug) from NIH 3T3, TCMK-1, 4T1, CT26.WT, and rat C6 cells. Antibodies: Affinity purified rabbit anti-KAP-1 antibody used for WB at 1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes.")
![Immunohistochemistry-Paraffin: KAP1 Antibody [NB500-158] - FFPE sections of human breast carcinoma. KAP1 antibody Lot3 (left) and Lot2 (right) used at a dilution of 1:1000 (1 ug/mL). Detection: DAB.](http://images.novusbio.com/fullsize/KAP1-Antibody-Immunohistochemistry-NB500-158-img0022.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: KAP1 Antibody [NB500-158] - Detection of Human KAP1 by Western blot. Whole cell lysate from HeLa (5, 15 and 50 ug), and 293T (50 ug) cells. KAP1 antibody at 0.1 ug/mL. Detection by chemiluminescence with an exposure time of 30 seconds.](http://images.novusbio.com/fullsize/KAP1-Antibody-Western-Blot-NB500-158-img0024.jpg)
![Western Blot: KAP1 Antibody [NB500-158] - Hep3B human hepatocellular carcinoma cell line. 50 ug cell lysate per lane. 10% SDS-PAGE. KAP1 (TRIM28) antibody at 1:1000 dilution in 5% milk at 4C O/N. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/KAP1-Antibody-Western-Blot-NB500-158-img0025.jpg)
![<b>Independent Antibodies Validation. </b>Immunoprecipitation: KAP1 Antibody [NB500-158] - Detection of human KAP-1 by western blot of immunoprecipitates. Samples: Whole cell lysate (1 mg for IP; 20% of IP loaded) from HeLa cells. Antibodies: Affinity purified rabbit anti-KAP-1 antibody NB500-158 (lot NB500-158-3) used for IP at 6 ug/mg lysate. KAP-1 was also immunoprecipitated by a previous lot of this antibody (lot NB500-158-2) and rabbit anti-KAP-1 antibody NB500-159. For blotting immunoprecipitated KAP-1, NB500-158 was used at 1 ug/ml. Detection: Chemiluminescence with an exposure time of 30 seconds.](http://images.novusbio.com/fullsize/KAP1-Antibody-Immunoprecipitation-NB500-158-img0026.jpg)
![Western Blot: hnRNP L Antibody (4D11) [NB120-6106] - analysis of hnRNP L in HEK whole cell lysate using anti-hnRNP L antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/hnRNP-L-Antibody-4D11-Western-Blot-NB120-6106-img0005.jpg "Western Blot: hnRNP L Antibody (4D11) [NB120-6106] - analysis of hnRNP L in HEK whole cell lysate using anti-hnRNP L antibody. Image from verified customer review.")
![Immunocytochemistry/Immunofluorescence: hnRNP L Antibody (4D11) [NB120-6106] - hnRNP L antibody was tested in HeLa cells at 5 ug/ml using a Dylight 488 conjugated secondary antibody (Green). Actin (Red) and DNA (Blue) were counterstained using Phalloidin 568 and DAPI.](http://images.novusbio.com/fullsize/hnRNP-L-Antibody-4D11-Immunocytochemistry-Immunofluorescence-NB120-6106-img0004.jpg)
![Immunohistochemistry-Frozen: hnRNP L Antibody (4D11) [NB120-6106]](http://images.novusbio.com/fullsize/hnRNP-L-Antibody-4D11-Immunohistochemistry-Frozen-NB120-6106-img0002.jpg)
![Western Blot: hnRNP L Antibody (4D11) [NB120-6106] - Western blot for anti-hnRNP-L on HeLa cell extracts](http://images.novusbio.com/fullsize/hnRNP-L-Antibody-4D11-Western-Blot-NB120-6106-img0001.jpg)
![Western Blot: hnRNP L Antibody (4D11) [NB120-6106] - Whole cell protein from HeLa (lane 1), A431 (lane 2), NIH-3T3 (lane 3) and PC12 (lane 4) was separated by SDS-PAGE and transferred to PVDF membrane. The membrane was probed with Anti-hnRNP L at 1 ug/ml and detected with an HRP conjugated anti-mouse secondary antibody by chemiluminescence.](http://images.novusbio.com/fullsize/hnRNP-L-Antibody-4D11-Western-Blot-NB120-6106-img0003.jpg)