| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2331SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-37235SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP1-28667SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2379SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-82991-25ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB200-111SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-19167SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-05767SS | |||
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - High autophagosome concentration is consumed during early immortalized human mesenchymal stem cell differentiation. Immortalized human mesenchymal stem cells were differentiated under osteogenic conditions (see Materials and methods) and assayed for changes in LC3I and LC3II during a 72-hour window. Cells were differentiated under standard conditions (top) or with addition of 5 uM rapamycin (middle) or 5 nM bafilomycin (bottom) for the first 3 hours of differentiation to modulate autophagy. Immunoblots were performed for LC3 at the indicated time points to assess autophagosome degradation via relative changes in LC3II (lower band; 17 kDa). Studies were repeated three times with similar trends seen consistently. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0041.jpg "Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - High autophagosome concentration is consumed during early immortalized human mesenchymal stem cell differentiation. Immortalized human mesenchymal stem cells were differentiated under osteogenic conditions (see Materials and methods) and assayed for changes in LC3I and LC3II during a 72-hour window. Cells were differentiated under standard conditions (top) or with addition of 5 uM rapamycin (middle) or 5 nM bafilomycin (bottom) for the first 3 hours of differentiation to modulate autophagy. Immunoblots were performed for LC3 at the indicated time points to assess autophagosome degradation via relative changes in LC3II (lower band; 17 kDa). Studies were repeated three times with similar trends seen consistently. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Analysis in PFA fixed NIH/3T3 cells using anti-LC3A antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-2331-img0046.jpg)
![Immunohistochemistry: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Staining in mouse meniscus and cartilage. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunohistochemistry-NB100-2331-img0045.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Autophagy mobilized during differentiation of immortalized human mesenchymal stem cells (ihMSCs). Cultured ihMSCs were stimulated to undergo osteogenesis to form osteoblasts for 30 days at 21% and 4% oxygen. LC3I and LC3II levels were assessed via immunoblot every 10 days and normalized to beta-actin to derive average LC3II band densities. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25523618/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A Antibody - BSA Free-Western Blot-NB100-2331-img0047.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Autophagy mobilized during differentiation of immortalized human mesenchymal stem cells (ihMSCs). Cultured ihMSCs were stimulated to undergo osteogenesis to form osteoblasts for 30 days at 21% and 4% oxygen. LC3I and LC3II levels were assessed via immunoblot every 10 days and normalized to beta-actin to derive average LC3II band densities. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0036.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - This LC3A antibody Image shows Analysis in human cell lysates.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0037.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - This LC3A antibody Image shows analysis of heart tissue lysates from mice which were subjected or not to 48 hours of starvation. The signal was developed using ECL method and this LC3 antibody was found to detect both forms of LC3, i.e. LC3A and LC3B. As expected, the levels of LC3B form were higher in the heart tissue lysates from starved mice.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0039.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Detection of HRP conjugated autophagic LC3 in mouse ES cell lysate. The atg5-/- lane (ES cells, cultured to form embryonic bodies, that are deficient in conversion of LC3-1 to LC3-11) demonstrates the specificity of NB 100-2331, as there is no detection of LC3-11. Photo courtesy of Dr. Beth Levine, UT Southwestern Medical Center.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0040.jpg)
![Immunocytochemistry/Immunofluorescence: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - This LC3A antibody Image shows an analysis in HeLa cells using anti-LC3 antibody (red). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-2331-img0038.jpg)
![Immunocytochemistry/Immunofluorescence: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Left panel shows untreated HeLa cells. Right panel shows HeLa cells that were treated with 50 uM CQ overnight. 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-LC3A antibody at 5 ug/mL overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-2331-img0042.jpg)
![Immunohistochemistry: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Rapamycin increases autophagy in brains of PDAPP mice. Representative epifluorescent (c200x) image of hippocampal CA1 in control- and rapamycin-fed transgenic PDAPP mice stained with an anti-LC3 antibody. An increase in LC3-immunoreactive puncta was observed in CA1 projections of transgenic PDAPP mice following rapamycin administration. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0009979) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunohistochemistry-NB100-2331-img0043.jpg)
![Immunohistochemistry: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Analysis in mouse renal tissue. Image from verifed customer review.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunohistochemistry-NB100-2331-img0044.jpg)
![Simple Western: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Image shows a specific band for LC3 in 0.5 mg/mL of Neuro2A lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Simple-Western-NB100-2331-img0025.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Chronic, third window RIC increases the expression of autophagosome proteins, LC3I/II & Atg5.(A) Western blots for autophagy related signaling proteins. (B) Quantification of the protein fold change in 3W RIC compared to 3W controls. Values are means ± S.E.M. n = 6–8 per group. An (*) denotes a statistically significant difference (P10 larvae/sample). Lc3 c & e, or p62 & Optineurin d protein levels were detected in absence or presence of BafA1, c & d, or in the presence or absence of Mm e. Actin was used as a loading control. Western Blots were repeated three, c & d, or two e times with protein extracts derived from independent experiments. The Lc3II/Actin or p62/Actin & Optineurin/Actin ratio, normalized to the control sample, is indicated below the blots. f–g Representative confocal micrographs & quantification of GFP-Lc3 co-localization with Mm clusters in infected dram1∆19n/∆19n & dram1+/+ larvae. The top images f show the entire region of imaging, while the bottom images f′ & f″ show details of GFP-Lc3 colocalization of Mm clusters in dram1∆19n/∆19n & dram1+/+ larvae. The arrowheads indicate GFP-Lc3-positive Mm clusters. The data is accumulated from two independent experiments (≥15 larvae/group) & represented by scatter & boxplots as detailed in the “Methods” section. Scale bars, 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32332700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-31020241612632.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Optn or p62 deficiency affects autophagosome formation.(A) Workflow of the experiments shown in (B-G). Larvae were treated with 100 nM of Baf A1 for 12 h from 3.5 dpf. The GPF-Lc3 negative larvae were selected to assay autophagy activity by Western blot, the GFP-Lc3 positive larvae were collected to monitor autophagic activity using confocal imaging. The red square indicates the region for confocal imaging. (B) Level of basal autophagy in WT & mutant embryos in absence or presence of Baf A1. Protein samples were extracted from 4 dpf WT & mutant larvae (>10 embryos/sample). The blots were probed with antibodies against Lc3 & Actin as a loading control. Western blots were repeated at least three times with independent extracts. (C) Quantification of Lc3-II fold changes in WT & mutant embryos in absence or presence of Baf A1. Western blot band intensities were quantified by Lab Image. Data is combined from three independent experiments. (D) Representative confocal micrographs of GFP-Lc3 puncta present in the tail fin of optn+/+, optn delta 5n/ delta 5n, p62+/+ & p62 delta 37n/ delta 37n at 4 dpf. Scale bars, 10 μm. (E). Quantification of the number of GFP-Lc3 puncta in optn+/+, optn delta 5n/ delta 5n, p62+/+ & p62 delta 37n/ delta 37n larvae with & without Baf A1 treatment. Each larva was imaged at a pre-defined region of the tail fin (as indicated by the red boxed area in Fig3 A) (≥11 larvae/group). Results are accumulated from two independent experiments. ns, non-significant, *p10 larvae/sample). The blots were probed with antibodies against Lc3 & Actin as a loading control & Lc3-II/Lc3-I ratios are indicated below. Western blots were repeated twice with independent extracts. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30818338), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415541914.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - UBC9 is degraded by autophagy in epithelial cells.(A) Immunolocalization of UBC9 in ultrathin sections of HKs transduced with empty or HPV16 E6/E7 vectors. Original view (left) & higher magnification (right) of boxed regions. Gold particles are selectively enriched in autophagic structures highlighted by arrows. Scale bar = 1 μm. (B) Top: Representative WB of HaCaT cells treated with the indicated autophagic activators (left) & inhibitors (right). Activation of autophagy was monitored by the conversion of LC3 (LC3-I) to the lipidated LC3 (LC3-II) form, a marker of autophagosome production induced by autophagic stimuli [41]. LC3-II accumulation was used to verify autophagic impairment [41]. Bottom: normalized UBC9 expression. Data are expressed as fold over untreated cells. Bars represent means ± SEM of n = 4 different biological replicates. ns: not significant (Kruskal–Wallis one-way ANOVA with Dunn’s post hoc test) compared to vehicle control groups. (C) Representative WB analysis of U-2 OS or MCF7 cells treated with chloroquine. n = 3 different biological replicates. (D) Representative WB analysis of MCF7 cells transduced with scramble or ATG5 shRNA. The observed ATG5 band represents the ATG5-ATG12 conjugated form. LC3-I accumulation is reported to evidence autophagic deficiencies promoted by shATG5. n = 3 replicates of a single transduction. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006262), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415525247.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Dram1 is required for GFP-Lc3 targeting to Mm clusters.a, b Representative confocal micrographs & quantification of GFP-Lc3 puncta in dram1∆19n/∆19n & dram1+/+ larvae in an unstimulated situation (basal autophagy, a) & following BafA1 treatment b. Each larva was imaged at a pre-defined region of the tail fin (≥11 larvae/group). Results are accumulated from two independent experiments & represented by scatter & boxplots as detailed in the “Methods” section. ns non-significant, *p 10 larvae/sample). Lc3 c & e, or p62 & Optineurin d protein levels were detected in absence or presence of BafA1, c & d, or in the presence or absence of Mm e. Actin was used as a loading control. Western Blots were repeated three, c & d, or two e times with protein extracts derived from independent experiments. The Lc3II/Actin or p62/Actin & Optineurin/Actin ratio, normalized to the control sample, is indicated below the blots. f–g Representative confocal micrographs & quantification of GFP-Lc3 co-localization with Mm clusters in infected dram1∆19n/∆19n & dram1+/+ larvae. The top images f show the entire region of imaging, while the bottom images f′ & f″ show details of GFP-Lc3 colocalization of Mm clusters in dram1∆19n/∆19n & dram1+/+ larvae. The arrowheads indicate GFP-Lc3-positive Mm clusters. The data is accumulated from two independent experiments (≥15 larvae/group) & represented by scatter & boxplots as detailed in the “Methods” section. Scale bars, 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32332700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415541920.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Knockdown of FUT1 is associated with an increase in autophagic flux. (a) Immunoblot analysis of LC3-II & p62 levels in control & FUT1 knockdown cells. Total cell lysates from MCF-7 & T47D cells transfected with control or FUT1 siRNAs were collected at 120 & 96 h post-transfection, respectively. Equal amounts of cell lysates were then loaded in each lane & separated by SDS-PAGE. Immunoblot analysis was performed with LC3 & p62 antibodies. Actin was used as a loading control. The intensity of LC3-II & p62 protein bands on immunoblot were quantified & normalized to actin, & the relative levels of protein expression were expressed as fold change by setting the control group value to 1. Values shown are mean±S.E.M. of three independent experiments (***P100 cells per group (*P<0.05) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27560716), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-31020241553512.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Effect of MIR376A overexpression on autophagy.(A) MCF-7 cells were co-transfected with either MIR-CNT (control plasmid) or MIR376A & GFP-LC3 plasmid, & GFP-LC3 dot formation was analyzed. White arrows indicate clusters of the GFP-LC3 dots in cells. (B) Quantification of the experiments in A. MIR376A overexpression, but not MIR-CNT expression, blocked starvation (STV)-induced autophagy (mean ± S.D. of independent experiments, n = 4, ***p<0,01). NON STV, non-starved (C) Overexpression of MIR376A resulted in a decrease in the autophagic activity of MCF-7 cells. Starvation-induced conversion of LC3-I to LC3-II in MCF-7 cells was analyzed. Tests were performed in the presence or absence of E64d (10 µg/ml) & Pepstatin A (10 µg/ml) (E+P). LC3-II/LC3-I densitometric ratios were marked. ACTB was used as a loading control. (D) MIR376A blocked starvation induced SQSTM1 degradation in MCF-7 cells. ACTB was used as a loading control. SQSTM1/ACTIN densitometric ratios were marked. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24358205), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415535132.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Tau clearance in vivo & autophagy function. Clearance kinetics of photoconverted Dendra-tau measured in neurons of WT-tau & AT152T-tau fish. Measurement of intensity of red Dendra-tau signal over time reflects the clearance or degradation of tau protein. (C–F) WBs for LC3-II, a well-characterized marker of autophagosome number, demonstrate that there no differences in levels of this protein between WT-tau & A152T-tau fish either at 24 hpf (pre-phenotype; C & D) or 72 hpf (post-phenotype; E & F). (E & F) Measurements of LC3-II levels in presence or absence of ammonium chloride provides a method for measuring autophagic flux. No differences observed between the two transgenic lines at 3 dpf, suggesting that autophagy functions normally in both WT-tau & A152T-tau fish (graph represents mean ± SD of four independent clutches per group for E & F & 3for C & D; two-tailed t-test). Image collected & cropped by CiteAb from the following publication (//academic.oup.com/brain/article/140/4/1128/2980948), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-31020241682110.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)
![Western Blot: Vimentin Antibody [NB300-223] - Analysis of tissue and cell lysates. Antibody at 1:5000 in red. [1] protein standard (red), [2] rat whole brain lysate, [3] HeLa, [4] SH-SY5Y, [5] HEK293, and [6] NIH-3T3 cell lysates. NB300-223 binds to the vimentin protein showing a single band at ~50 kDa. The blot was simultaneously probed with mouse mAb to MAP2C/D, dilution 1:5000 in green, revealing multiple bands around 280 kDa that correspond to full length MAP2A/2B isotypes, and ~70 kDa bands which are MAP2C/D isotypes. MAP2 isotypes are seen only in extracts containing neuronal lineage cells.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Western-Blot-NB300-223-img0002.jpg "Western Blot: Vimentin Antibody [NB300-223] - Analysis of tissue and cell lysates. Antibody at 1:5000 in red. [1] protein standard (red), [2] rat whole brain lysate, [3] HeLa, [4] SH-SY5Y, [5] HEK293, and [6] NIH-3T3 cell lysates. NB300-223 binds to the vimentin protein showing a single band at ~50 kDa. The blot was simultaneously probed with mouse mAb to MAP2C/D, dilution 1:5000 in green, revealing multiple bands around 280 kDa that correspond to full length MAP2A/2B isotypes, and ~70 kDa bands which are MAP2C/D isotypes. MAP2 isotypes are seen only in extracts containing neuronal lineage cells.")
![Immunohistochemistry: Vimentin Antibody [NB300-223] - Attenuated reactive astrocytosis after stroke in Smad1 cKO mice. Enlarged IHC images of boxed areas at the cortical peri-infarct area with the indicated reactive astrocyte markers GFAP, Nestin, and Vimentin. Enlarged images of GFAP IHC highlight the hypertrophic morphology of GFAP+ astrocytes in mutants. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0136967), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunohistochemistry-NB300-223-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: Vimentin Antibody [NB300-223] - Human A7 cells. Cells were fixed with 10% formalin and permeabilized with 0.1% TritonX-100. After blocking, cells were incubated with primary antibody (1:600) at 4C O/N followed with Alexa Fluor 488 labeled secondary antibody and counterstained with DAPI and Phalloidin for nuclei and F-actin respectively. Imaged with Leica TCS SP5 confocal microscope. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunocytochemistry-Immunofluorescence-NB300-223-img0004.jpg)
![Immunohistochemistry: Vimentin Antibody [NB300-223] - Increased numbers of differentiating NSPCs in SVZ of G93A-SOD1 brain. Confocal microscopy images of dorsal and ventral regions of SVZ in G93A-SOD1 and Wt-SOD1 brain at postnatal week 18, stained for nestin (green), GFAP (red), and vimentin (blue). Scale bar = 50 um. Image collected and cropped by CiteAb from the following publication (//www.molecularbrain.com/content/8/1/5), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunohistochemistry-NB300-223-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: Vimentin Antibody [NB300-223] - Comparative analysis of epithelial and mesenchymal markers expressions. Fluorescence immunocytochemistry staining for E-cadherin (green), N-cadherin (red) and vimentin (cyan) was performed on esophageal cancer cells under static and microfluidic flow conditions at different time points. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep38221), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunocytochemistry-Immunofluorescence-NB300-223-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: Vimentin Antibody [NB300-223] - Analysis of HeLa cell culture. Antibody at 1:10,000 in green, and costained with mouse mAb to actin, dilution 1:500 in red. The blue is DAPI staining of nuclear DNA. The vimentin antibody stains the intermediate filament network while the actin antibody labels the submembranous cytoskeleton, stress fibers, and bundles of actin associated with cell adhesion sites.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunocytochemistry-Immunofluorescence-NB300-223-img0001.jpg)
![Immunohistochemistry-Frozen: Vimentin Antibody [NB300-223] - 10 um Cryosections from PFA fixed murine brain acute slices stained with Vimentin antibody (1:600) and Alexa Fluor 488 anti chicken IgG. Antibody showed specific staining, also of blood vessels. IHC-Fr image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunohistochemistry-Frozen-NB300-223-img0003.jpg)
![Immunohistochemistry-Frozen: Vimentin Antibody [NB300-223] - Infarcted mouse heart frozen sections stained with vimentin antibody at 1:200. Secondary antibody at 1:500. Fixation with 4% PFA. IHC-Fr image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Vimentin-Antibody-Immunohistochemistry-Frozen-NB300-223-img0005.jpg)
![Immunocytochemistry/ Immunofluorescence: Vimentin Antibody [NB300-223] - Increased numbers of differentiating NSPCs in SVZ of G93A-SOD1 brain. (A) Confocal microscopy images of dorsal & ventral regions of SVZ in G93A-SOD1 & Wt-SOD1 brain at postnatal week 18, stained for nestin (green), GFAP (red), & vimentin (blue). Scale bar = 50 μm. (B) Quantification of nestin-, GFAP-, & vimentin-positive cells in SVZ of G93A-SOD1 & Wt-SOD1 mice. Data are means ± SD of 3 mice per group. **p 20 days (PyMT-1099 LT) were injected orthotopically into mammary fat pads of NSG mice. The graph represents tumor growth in PyMT-1099 & PyMT-1099 LT group of mice. (B) Histological tumor sections from tumors of PyMT-1099 or PyMT-1099 LT cells described in (A) were stained with H&E to assess the morphology of primary tumors. Representative microphotographs are shown from tumors of 2 out of the 6 mice used in the experiment. (C) Immunofluorescence analysis was performed to assess the expression of the EMT markers FN1, VIM, E-CAD & N-CAD in tumors formed by PyMT-1099 or PyMT-1099 LT cells in the experiment described in (A). DAPI was used as a nuclear counterstain. Representative pictures are shown from tumors of 2 out of the 6 mice used in the experiment. Scale bar, 100 μm. (D) The graph represents the number of lung metastases formed in NSG mice orthotopically transplanted with PyMT-1099 or PyMT-1099 LT cells; n = 6. (E) The graph represents the number of lung metastases formed in NSG mice injected with PyMT-1099 or PyMT-1099 LT cells through the tail vein; n = 6. The mice were sacrificed 8 weeks post-injection, & lungs were resected for the analysis of cancer cell colonization/ metastases formation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30108334), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-223_chicken-polyclonal-vimentin-antibody-31020241621828.jpg)
![Immunohistochemistry-Paraffin: SOX2 Antibody [NB110-37235] - Staining of human uterus, endometrial glands.](http://images.novusbio.com/fullsize/SOX2-Antibody-Immunohistochemistry-Paraffin-NB110-37235-img0012.jpg)
![Western Blot: SOX2 Antibody [NB110-37235] - Detection of SOX2 in mouse brain lysate using NB110-37235 at 0.5 ug/mL.](http://images.novusbio.com/fullsize/SOX2-Antibody-Western-Blot-NB110-37235-img0008.jpg)
![Flow Cytometry: SOX2 Antibody [NB110-37235] - An intracellular stain was performed on A549 with NB110-37235 and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylgiht 550.](http://images.novusbio.com/fullsize/SOX2-Antibody-Flow-Cytometry-NB110-37235-img0015.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: SOX2 Antibody [NB110-37235] - MDA-MB-231 subclones transfected with NTC or HIF-1 alpha shRNA vector were treated with vehicle (V) or paclitaxel (P) and immunoblot assay was performed. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/SOX2-Antibody-Western-Blot-NB110-37235-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: SOX2 Antibody - BSA Free [NB110-37235] - Rat FR 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 SOX2 Antibody (NB110-37235) at 2ug/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/SOX2-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-37235-img0019.jpg)
![Flow Cytometry: SOX2 Antibody - BSA Free [NB110-37235] - An intracellular stain was performed on U-251 MG cells with SOX2 Antibody NB110-37235 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/SOX2-Antibody---BSA-Free-Flow-Cytometry-NB110-37235-img0020.jpg)
![Western Blot: SOX2 Antibody [NB110-37235] - Expression of pluripotency factor Sox2 in human head and neck cancer cell lines FaDu and HN5. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/SOX2-Antibody-Western-Blot-NB110-37235-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: SOX2 Antibody [NB110-37235] - Staining of SOX2 in NTERA2 cells with Dylight 488 (Green). Alpha-tubulin and nuclei were counterstained with Dylight 550 (Red) and DAPI (Blue), respectively.](http://images.novusbio.com/fullsize/SOX2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-37235-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: SOX2 Antibody [NB110-37235] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-SOX2 (NB110-37235) 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-stain at a 1:1000 dilution and detected with and anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/SOX2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-37235-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: SOX2 Antibody - BSA Free [NB110-37235] - NIH3T3 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 SOX2 Antibody (NB110-37235) at 2ug/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/SOX2-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-37235-img0018.jpg)
![Immunohistochemistry: Olig2 Antibody [NBP1-28667] - Mouse cerebral microslice section (coronal, P14) was co-immunostained with anti-Olig2 and anti-NeuN antibodies. Green: Olig2, Red: NeuN. Anti-Olig2 was used at a 1:800 dilution. This image was submitted via customer Review.](http://images.novusbio.com/fullsize/Olig2-Antibody-Immunohistochemistry-NBP1-28667-img0005.jpg "Immunohistochemistry: Olig2 Antibody [NBP1-28667] - Mouse cerebral microslice section (coronal, P14) was co-immunostained with anti-Olig2 and anti-NeuN antibodies. Green: Olig2, Red: NeuN. Anti-Olig2 was used at a 1:800 dilution. This image was submitted via customer Review.")
![Immunocytochemistry/Immunofluorescence: Olig2 Antibody [NBP1-28667] - Rat cortical neuroepithelial cells with anti-Olig2 (red). The cells were treated with basic FGF for 30 hours prior to staining (this induces Olig2 expression in these primary cells).](http://images.novusbio.com/fullsize/Olig2-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-28667-img0004.jpg)
![Immunohistochemistry-Frozen: Olig2 Antibody [NBP1-28667] - Mouse brain cortex. Antibody at 1:300. Purple: Olig2. Green: CD31. Image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Olig2-Antibody-Immunohistochemistry-Frozen-NBP1-28667-img0006.jpg)
![Western Blot: OCT4 Antibody [NB100-2379] - YM155 significantly reduced tumorsphere formation and inhibited EGFR autophosphorylation and G9a expression. YM155 is reported to suppress cancer stemness; therefore, we used this compound to investigate the cellular mechanism of tumorsphere formation. To compare the cytotoxic capacity of YM155 against tumorsphere formation and parental cell lines, YM155 was applied to HCC827 and A549 cells in the stemness cultured or integrated medium. (F) Moreover, YM155 inhibited EGFR autophosphorylation in A549-derived tumorspheres and reduced Oct4 expression. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0182149) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OCT4-Antibody-Western-Blot-NB100-2379-img0014.jpg "Western Blot: OCT4 Antibody [NB100-2379] - YM155 significantly reduced tumorsphere formation and inhibited EGFR autophosphorylation and G9a expression. YM155 is reported to suppress cancer stemness; therefore, we used this compound to investigate the cellular mechanism of tumorsphere formation. To compare the cytotoxic capacity of YM155 against tumorsphere formation and parental cell lines, YM155 was applied to HCC827 and A549 cells in the stemness cultured or integrated medium. (F) Moreover, YM155 inhibited EGFR autophosphorylation in A549-derived tumorspheres and reduced Oct4 expression. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0182149) licensed under a CC-BY license.")
![Western Blot: OCT4 Antibody [NB100-2379] - WB detection of OCT4 in mouse brain lysate using OCT4 antibody with ECL based detection. The antibody generated a specific band of OCT4 at the expected ~40kDa position.](http://images.novusbio.com/fullsize/OCT4-Antibody-Western-Blot-NB100-2379-img0011.jpg)
![Flow Cytometry: OCT4 Antibody [NB100-2379] - An intracellular stain was performed on Jurkat with NB100-2379 and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.](http://images.novusbio.com/fullsize/OCT4-Antibody-Flow-Cytometry-NB100-2379-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: OCT4 Antibody [NB100-2379] - Ntera2 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- NB100-2379 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 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/OCT4-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2379-img0018.jpg)
![Western Blot: OCT4 Antibody [NB100-2379] - MDA-MB-231 subclones transfected with NTC or HIF-1 alpha shRNA vector were treated with vehicle (V) or paclitaxel (P) and Western blot assay was performed. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/OCT4-Antibody-Western-Blot-NB100-2379-img0016.jpg)
![Immunohistochemistry-Paraffin: OCT4 Antibody [NB100-2379] - Analysis of a FFPE tissue section of mouse brain using 1:200 dilution of OCT4 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/OCT4-Antibody-Immunohistochemistry-Paraffin-NB100-2379-img0017.jpg)
![Flow Cytometry: OCT4 Antibody - BSA Free [NB100-2379] - An intracellular stain was performed on U2-OS cells with OCT4 NB100-2379AF647 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/OCT4-Antibody---BSA-Free-Flow-Cytometry-NB100-2379-img0022.jpg)
![Western Blot: OCT4 Antibody [NB100-2379] - The expression of pluripotency factors Oct4 in human head and neck cancer cell lines.](http://images.novusbio.com/fullsize/OCT4-Antibody-Western-Blot-NB100-2379-img0013.jpg)
![Flow Cytometry: OCT4 Antibody [NB100-2379] - An intracellular stain was performed on Jurkat cells with OCT4 Antibody NB100-2379 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/OCT4-Antibody-Flow-Cytometry-NB100-2379-img0019.jpg)
![Flow Cytometry: OCT4 Antibody [NB100-2379] - An intracellular stain was performed on Neuro2a cells with OCT4 Antibody NB100-2379 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/OCT4-Antibody-Flow-Cytometry-NB100-2379-img0020.jpg)
![Flow Cytometry: OCT4 Antibody [NB100-2379] - An intracellular stain was performed on Ntera2 cells with OCT4 Antibody NB100-2379 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/OCT4-Antibody-Flow-Cytometry-NB100-2379-img0021.jpg)
![Western Blot: OCT4 Antibody - BSA Free [NB100-2379] - Protein expression of NANOG a, OCT4 b & SOX2 c in bovine uterine tissues obtained from control cows & from cows with adenomyosis. Data were normalized against glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Bars represent the mean ± SEM. There were no statistical differences between uterine normal & adenomyotic tissues (P > 0.05), as determined by Student’s t-test. Representative blots for NANOG, OCT4, SOX2 & GAPDH are shown below the graphs d. MM – molecular weight marker, C – tissues obtained from control cows, ADENO – tissues obtained from cows with adenomyosis Image collected & cropped by CiteAb from the following publication (//www.rbej.com/content/13/1/110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2379_rabbit-polyclonal-oct4-antibody-310202415394524.jpg)
![Western Blot: OCT4 Antibody - BSA Free [NB100-2379] - Protein expression of pluripotency markers in uterine cells isolated from control cows & from cows with adenomyosis. NANOG a OCT4 b & SOX2 c protein expression in uterine stromal cells. NANOG d OCT4 e & SOX2 f protein expression in uterine myometrial cells. Data were normalized against glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Bars represent the mean ± SEM. Asterisks indicate statistical differences between uterine normal & adenomyotic tissue (*P < 0.05; **P < 0.01), as determined by Student’s t-test. Representative blots for NANOG, OCT4, SOX2 & GAPDH are shown below the graphs g. MM – molecular weight marker, C – cells obtained from control cows, ADENO – cells obtained from cows with adenomyosis Image collected & cropped by CiteAb from the following publication (//www.rbej.com/content/13/1/110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2379_rabbit-polyclonal-oct4-antibody-310202415384144.jpg)
![Western Blot: NF-H Antibody [NB300-135] - Proof of viability of organotypic adult brain slices. Brain slices of adult 9 month old wildtype (WT) mice were dissected fresh or incubated for either 1 day or for 14 days to examine vitality of slices (A). Brain slices were subsequently analyzed by Western blot using antibodies against Neurofilament-200 kDa, total tau (Tau-5) and actin served as a control. Size markers are given as kDa on the right side. Note some degradation of neurofilament but stability of Tau-5. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnagi.2018.00113/full) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NF-H-Antibody-Western-Blot-NB300-135-img0004.jpg "Western Blot: NF-H Antibody [NB300-135] - Proof of viability of organotypic adult brain slices. Brain slices of adult 9 month old wildtype (WT) mice were dissected fresh or incubated for either 1 day or for 14 days to examine vitality of slices (A). Brain slices were subsequently analyzed by Western blot using antibodies against Neurofilament-200 kDa, total tau (Tau-5) and actin served as a control. Size markers are given as kDa on the right side. Note some degradation of neurofilament but stability of Tau-5. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnagi.2018.00113/full) licensed under a CC-BY license.")
![Immunohistochemistry: NF-H Antibody [NB300-135] - Mouse hippocampus section stained with rabbit pAb to NF-H, dilution 1:2,000 in red, and costained with mouse mAb to myelin basic protein (MBP), dilution 1:5,000 in green. The blue is DAPI staining of nuclear DNA. Following transcardial perfusion with 4% paraformaldehyde, brain was post fixed for 24 hours, cut to 45uM, and free-floating sections were stained with above antibodies. The NF-H antibody labels a network of axons of different neurons, while the MBP antibody stains myelin sheath around these axons.](http://images.novusbio.com/fullsize/NF-H-Antibody-Immunohistochemistry-NB300-135-img0002.jpg)
![Immunohistochemistry: NF-H Antibody [NB300-135] - Immunostainings of adult organotypic brain slices at the hippocampal level. Brain slices were prepared from WT or TG adult mice and incubated with okadaic acid (OA). Brain slices were stained for nuclear DAPI (blue, A,B) showing intact brain structures. Thiazine Red staining (C,D) shows red fluorescent plaques in the hippocampus (D) of TG mice, while only background is seen in the hippocampus (C) of WT mice. Staining of neurofilament fibers (G,H) shows good neuronal viability both in WT and TG mice. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnagi.2018.00113/full) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NF-H-Antibody-Immunohistochemistry-NB300-135-img0005.jpg)
![Western Blot: NF-H Antibody [NB300-135] - Analysis of 200kDa Neurofilament Heavy expression in rat spinal cord extract. The first lane is Coomassie Brilliant Blue stained and the second lane is probed with rabbit anti-Neurofilament Heavy antibody NB300-135. The NF-H corresponds to a weight of 200kDa.](http://images.novusbio.com/fullsize/200kDa-Neurofilament-Heavy-Antibody-Western-Blot-NB300-135-img0001.jpg)
![Western Blot: NF-H Antibody [NB300-135] - Different tissue lysates using rabbit pAb to NF-H, dilution 1:10,000 in green: [1] protein standard (red), [2] rat brain, [3] rat spinal cord [4] mouse brain, and [5] mouse spinal cord lysate. Strong band at about 220 kDa corresponds to the phosphorylated axonal form of the NF-H subunit. Smaller proteolytic fragments of NF-H are also detected with RPCA-NF-H antibody.](http://images.novusbio.com/fullsize/NF-H-Antibody-Western-Blot-NB300-135-img0003.jpg)
![Western Blot: ZEB2 Antibody [NBP1-82991] - Analysis in human cell lines SK-MEL-30 and Caco-2 using Anti-ZEB2 antibody. Corresponding ZEB2 RNA-seq data are presented for the same cell lines. Loading control: Anti-HDAC1.](http://images.novusbio.com/fullsize/ZEB2-Antibody-Western-Blot-NBP1-82991-img0013.jpg "<b>Orthogonal Strategies Validation. </b>Western Blot: ZEB2 Antibody [NBP1-82991] - Analysis in human cell lines SK-MEL-30 and Caco-2 using Anti-ZEB2 antibody. Corresponding ZEB2 RNA-seq data are presented for the same cell lines. Loading control: Anti-HDAC1.")
![<b>Orthogonal Strategies Validation. </b>Western Blot: ZEB2 Antibody [NBP1-82991] - Depletion of TRIM14 increased ZEB2 polyubiquitination and proteasomal degradation. Western blot analysis of TRIM14, ZEB2 and beta-actin in LN229 and U251 cells transduced with the indicated shRNA in the absence or presence of 10uM MG132. Image collected and cropped by CiteAb from the following publication (//jeccr.biomedcentral.com/articles/10.1186/s13046-019-1070-x), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ZEB2-Antibody-Western-Blot-NBP1-82991-img0018.jpg)
![Immunohistochemistry-Paraffin: ZEB2 Antibody [NBP1-82991] - Staining of human pancreas shows no positivity as expected.](http://images.novusbio.com/fullsize/ZEB2-Antibody-Immunohistochemistry-Paraffin-NBP1-82991-img0017.jpg)
![Immunohistochemistry-Paraffin: ZEB2 Antibody [NBP1-82991] - Staining of human cerebral cortex shows moderate nuclear positivity in glial cells.](http://images.novusbio.com/fullsize/ZEB2-Antibody-Immunohistochemistry-Paraffin-NBP1-82991-img0014.jpg)
![Immunohistochemistry-Paraffin: ZEB2 Antibody [NBP1-82991] - Staining of human colon shows moderate nuclear positivity in a subset of lymphoid cells.](http://images.novusbio.com/fullsize/ZEB2-Antibody-Immunohistochemistry-Paraffin-NBP1-82991-img0015.jpg)
![Immunohistochemistry-Paraffin: ZEB2 Antibody [NBP1-82991] - Staining of human glioma shows moderate nuclear positivity in tumor cells.](http://images.novusbio.com/fullsize/ZEB2-Antibody-Immunohistochemistry-Paraffin-NBP1-82991-img0016.jpg)
![SU5402, FGFR1 inhibitor, affects the EMT transcription factors.(A, B) ERK1/2 phosphorylation (p-ERK1/2) was determined by immunoblotting in HSC-4 & OTC-04 treated for 30 min with 30 ng/ml FGF2 or 30 ng/ml FGF7 in presence of 10% FBS (A) & in TSU & HOC313 cells treated for 1 h with 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 with TGF-beta , NMuMG cells underwent EMT with the IIIc-isoform of FGFR1[17]. After NMuMG cells pretreated with TGF-beta were transfected with mouse Fgfr1 siRNA or treated with SU5402, the cells were further incubated in culture medium (CM) from TSU cells. SU, SU5402; siFR1, siRNA against mouse Fgfr1. (D)FGF2 mRNA levels were determined by RT-qPCR analyses. The ratio of FGF2 mRNA to GAPDH mRNA in HSC-4 cells was 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 were 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 was determined by RT-qPCR (F) & immunoblot (G) analyses, following treatment with 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 were determined by Student’s t-test. **p < 0.01. (H) TSU cells treated with 10 μM U0126 in absence of FBS were subjected to immunoblotting with the indicated antibodies. alpha -tubulin was 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/nbp1-82991_rabbit-polyclonal-zeb2-antibody-21020242345489.jpg)
![Western Blot: ZEB2 Antibody [NBP1-82991] - ZEB2 is a downstream target of TRIM14. a Western blot analysis of TRIM14, EMT related biomarks (Snail1, Twist1, ZEB1, ZEB2 & SLUG), & beta -actin in LN229 & U251 cells transfected with shTRIM14–1, shTRIM14–2 or control shRNA. b Western blot analysis of TRIM14, N-cadherin, E-cadherin, Vimentin & beta -actin in LN229 & U251 cells transduced with the indicated plasmid. c Representative images of transwell invasion assay using LN229 & U251 cells transfected with the indicated plasmid. Quantification of transwell invasion assay is shown. ***p < 0.001; n = 3 experiment. d Representative images of wound healing assay using LN229 & U251 cells with the indicated plasmid. Quantification of wound healing assay is shown. ***p < 0.001, n = 3 experiments. e Representative images of 3D spheroid BME cell invasion assays using LN229 & U251 cells with the indicated plasmid. Quantification of 3D spheroid BME cell invasion assays is shown. ***p < 0.001, n = 3 experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30728039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-82991_rabbit-polyclonal-zeb2-antibody-310202416121912.jpg)
![Western Blot: ZEB2 Antibody [NBP1-82991] - TRIM14 function was demonstrated in vivo & IHC. a ShCtrl-transplanted & shTRIM14-transplanted LN229 cells were counted & transplanted in orthotopic nude mice model respectively, n = 6. b Survival curve of shCtrl-transplanted or shTRIM14-transplanted intracranial xenografts. ***, P < 0.001, n = 6. c Representative pseudocolour bioluminescence images of orthotopic tumours bearing control or TRIM14-depleted LN229 cells on the days as indicated. Quantification of tumor volume is shown. ***p < 0.001; n = 3 experiment. d The HE assay was performed to show tumor cytostructure. e Western blot analysis of TRIM14 & ZEB2 extracted from four pairs mice from shCtrl-transplanted group & shCtrl-transplanted group. Equal loading is confirmed by beta -actin levels. f IHC staining of TRIM14 & ZEB2 in four representative GBM specimens Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30728039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-82991_rabbit-polyclonal-zeb2-antibody-310202416113532.jpg)
![Western Blot: ZEB2 Antibody [NBP1-82991] - ZEB2 is involved in the function of TRIM14. a Western blot analysis of TRIM14, EMT related biomarks (Snail1, Twist1, ZEB1, ZEB2 & SLUG), & beta -actin in HS683 & U87 cells transfected with vector or TRIM14. b Western blot analysis of TRIM14, N-cadherin, E-cadherin, Vimentin & beta -actin in HS683 & U87 cells transduced with the indicated plasmid. c Representative images of transwell invasion assay using HS683 & U87 cells transfected with the indicated plasmid. Quantification of transwell invasion assay is shown. ***p < 0.001; n = 3 experiment. d Representative images of wound healing assay using HS683 & U87 cells with the indicated plasmid. Quantification of wound healing assay is shown. ***p < 0.001, n = 3 experiments. e Representative images of 3D spheroid BME cell invasion assays using HS683 & U87 cells with the indicated plasmid. Quantification of 3D spheroid BME cell invasion assays is shown. ***p < 0.001, n = 3 experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30728039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-82991_rabbit-polyclonal-zeb2-antibody-310202416121955.jpg)
![Western Blot: USP7 Antibody [NB100-513] - Samples: Wholecell lysate (10 ug) from HEK293T, RKO, Hep-G2, Jurkat,HeLa, TCMK-1, and NIH 3T3 cells prepared using NETNlysis buffer. Antibody: Affinity purified rabbit anti-USP7antibody used for WB at0.04 ug/ml. Detection: Chemiluminescence with anexposure time of 10 seconds](http://images.novusbio.com/fullsize/USP7-Antibody-Western-Blot-NB100-513-img0004.jpg "Western Blot: USP7 Antibody [NB100-513] - Samples: Wholecell lysate (10 ug) from HEK293T, RKO, Hep-G2, Jurkat,HeLa, TCMK-1, and NIH 3T3 cells prepared using NETNlysis buffer. Antibody: Affinity purified rabbit anti-USP7antibody used for WB at0.04 ug/ml. Detection: Chemiluminescence with anexposure time of 10 seconds")
![Immunohistochemistry-Paraffin: USP7 Antibody [NB100-513] - Sample: FFPE section of human ovarian carcinoma.Antibody: Affinity purified rabbit anti-USP7 used at 1:5,000 (0.2ug/ml). Detection:DAB](http://images.novusbio.com/fullsize/USP7-Antibody-Immunohistochemistry-Paraffin-NB100-513-img0002.jpg)
![Immunohistochemistry-Paraffin: USP7 Antibody [NB100-513] - Sample: FFPE section of mouse renal cell carcinoma.Antibody: Affinity purified rabbit anti-USP7 used at 1:5,000 (0.2ug/ml). Detection:DAB](http://images.novusbio.com/fullsize/USP7-Antibody-Immunohistochemistry-Paraffin-NB100-513-img0001.jpg)
![Immunoprecipitation: USP7 Antibody [NB100-513] - Samples: Wholecell lysate (10 ug) from HEK293T, RKO, Hep-G2, Jurkat,HeLa, TCMK-1, and NIH 3T3 cells prepared using NETNlysis buffer. Antibody: Affinity purified rabbit anti-USP7antibody used for WB at0.04 ug/ml. Detection: Chemiluminescence with anexposure time of 10 seconds](http://images.novusbio.com/fullsize/USP7-Antibody-Immunoprecipitation-NB100-513-img0003.jpg)
![Western Blot: p14ARF/CDKN2A Antibody [NB200-111] - Inhibition of AKT decreases p53mut stability. T24 cells were transfected with non-targeting control, AKT1, or p14ARF siRNA. Cells were treated with NCS348884 (4 i1/4M), Nutlin3A (5 i1/4M) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. Image collected and cropped by Citeab from the following publication (AKT regulates NPM dependent ARF localization and p53mut stability in tumors. Oncotarget (2014)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Western-Blot-NB200-111-img0012.jpg "<b>Genetic Strategies Validation. </b>Western Blot: p14ARF/CDKN2A Antibody [NB200-111] - Inhibition of AKT decreases p53mut stability. T24 cells were transfected with non-targeting control, AKT1, or p14ARF siRNA. Cells were treated with NCS348884 (4 i1/4M), Nutlin3A (5 i1/4M) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. Image collected and cropped by Citeab from the following publication (AKT regulates NPM dependent ARF localization and p53mut stability in tumors. Oncotarget (2014)) licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Immunohistochemistry: p14ARF/CDKN2A Antibody [NB200-111] - Inhibition of AKT modulates p53 stability in-vivo and synergizes with ionizing radiation to inhibit tumor growth( Sections of PSN1 xenografts treated with three consecutive doses of MK-2206 (60 mg/kg). Sections of PSN1 xenografts and in-vitro PSN1 cells fixed and stained with anti-NPM (red) and anti-p14ARF (green). Image collected and cropped by Citeab from the following publication (AKT regulates NPM dependent ARF localization and p53mut stability in tumors. Oncotarget (2014)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Immunocytochemistry-Immunofluorescence-NB200-111-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: p14ARF/CDKN2A Antibody [NB200-111] - p14ARF antibody was tested in HeLa cells with Dylight 488 (green). Nuclei were counterstained with DAPI (blue). Tubulin was stained with alpha tubulin (red).](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Immunocytochemistry-Immunofluorescence-NB200-111-img0006.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: p14ARF/CDKN2A Antibody [NB200-111] - ARF expression levels in OCI/AML3 cells after proteasome treatment. This image was submitted via customer Review.](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Western-Blot-NB200-111-img0009.jpg)
![Flow Cytometry: p14ARF/CDKN2A Antibody [NB200-111] - p14ARF antibody was tested at 1:400 in HeLa cells using an Alexa Fluor 488 secondary (shown in purple). M1 is defined by unstained cells.](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Flow-Cytometry-NB200-111-img0007.jpg)
![Western Blot: p14ARF/CDKN2A Antibody [NB200-111] - Analysis of HeLa Whole Cell Lysate (NB800-PC1) using p14ARF antibody (lot C) employing ECL detection method.](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Western-Blot-NB200-111-img0008.jpg)
![Immunohistochemistry-Frozen: p14ARF/CDKN2A Antibody [NB200-111] - Mouse brain section, hippocampal (10 um thickness). 3% PFA perfused. 1:1000 dilultion. Image from verified customer review. Image using the Biotin form of this antibody.](http://images.novusbio.com/fullsize/p14ARF-CDKN2A-Antibody-Immunohistochemistry-Frozen-NB200-111-img0010.jpg)
![Western Blot: p14ARF/CDKN2A Antibody - BSA Free [NB200-111] - Inhibition of AKT decreases p53mut stability(A) T24 cells & PSN1 cells were treated with MK-2206 (5 μM) or DMSO for 24 hrs. Cells were fixed & stained with DAPI & anti-mutant p53 (OP29 clone). (B) T24 cells were pre-treated with MK-2206 (5 μM) or DMSO for 24 hrs before the addition of fresh media containing cyclohexamide (100 μM) (CHX) in combination with MK-2206 (5 μM) or DMSO for the times indicated. Nuclear extracts were prepared from treated cells & blotted with the indicated antibodies. Quantification is relative to initiation of CHX treatment for both conditions *, MK-2206 is 40% of DMSO control but taken as 1.0 for relative assessment. (C) H1299 cells were transfected with HA-tagged-ubiquitin & mutant p53 (R175H or R248W) as indicated. Transfected cells were treated with DMSO, MK-2206 (5 μM) or Nutlin3A (5 μM) for 16hrs as indicated. p53 immunoprecipitates & whole cell lysates were probed with the indicated antibodies. (D) T24 cells were transfected with non-targeting control or p14ARF siRNA & treated with DMSO, MK-2206 (5 μM) or the NPM oligomerisation inhibitor NCS348884 (4 μM) (Qi et al., 2008) as indicated. (E) T24 cells were transfected with non-targeting control, AKT1, or p14ARF siRNA. Cells were treated with NCS348884 (4 μM), Nutlin3A (5 μM) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. (F) KPC mice derived KRASG12D p53 Floxed (p53Fl), KRASG12D p53R172H ARF+/+ & KRASG12D p53R172H ARF−/− pancreatic tumor cells were treated with MK-2206 (1μM), Nutlin3A (5μM) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25071014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb200-111_rabbit-polyclonal-p14arf-cdkn2a-antibody-310202416203719.jpg)
![Western Blot: p14ARF/CDKN2A Antibody - BSA Free [NB200-111] - Inhibition of AKT decreases p53mut stability(A) T24 cells & PSN1 cells were treated with MK-2206 (5 μM) or DMSO for 24 hrs. Cells were fixed & stained with DAPI & anti-mutant p53 (OP29 clone). (B) T24 cells were pre-treated with MK-2206 (5 μM) or DMSO for 24 hrs before the addition of fresh media containing cyclohexamide (100 μM) (CHX) in combination with MK-2206 (5 μM) or DMSO for the times indicated. Nuclear extracts were prepared from treated cells & blotted with the indicated antibodies. Quantification is relative to initiation of CHX treatment for both conditions *, MK-2206 is 40% of DMSO control but taken as 1.0 for relative assessment. (C) H1299 cells were transfected with HA-tagged-ubiquitin & mutant p53 (R175H or R248W) as indicated. Transfected cells were treated with DMSO, MK-2206 (5 μM) or Nutlin3A (5 μM) for 16hrs as indicated. p53 immunoprecipitates & whole cell lysates were probed with the indicated antibodies. (D) T24 cells were transfected with non-targeting control or p14ARF siRNA & treated with DMSO, MK-2206 (5 μM) or the NPM oligomerisation inhibitor NCS348884 (4 μM) (Qi et al., 2008) as indicated. (E) T24 cells were transfected with non-targeting control, AKT1, or p14ARF siRNA. Cells were treated with NCS348884 (4 μM), Nutlin3A (5 μM) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. (F) KPC mice derived KRASG12D p53 Floxed (p53Fl), KRASG12D p53R172H ARF+/+ & KRASG12D p53R172H ARF−/− pancreatic tumor cells were treated with MK-2206 (1μM), Nutlin3A (5μM) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25071014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb200-111_rabbit-polyclonal-p14arf-cdkn2a-antibody-310202416212372.jpg)
![Immunocytochemistry/ Immunofluorescence: p14ARF/CDKN2A Antibody - BSA Free [NB200-111] - Inhibition of AKT modulates p53 stability in-vivo & synergizes with ionizing radiation to inhibit tumor growth(A) PSN1 xenografts (PSN1 cells co-injected with LTC-14 stellate cells) established in the flank of athymic nude mice were treated with MK-2206 (60 mg/kg-320 mg/kg) as indicated or beta -cyclo-dextrin (1.5 mg/ml) carrier. Xenograft tumors were lysed & lysates probed by western blot with the indicated antibodies. (B-D) Sections of PSN1 xenografts treated with three consecutive doses of MK-2206 (60 mg/kg). (B) Sections of PSN1 xenografts & in-vitro PSN1 cells fixed & stained with anti-NPM (red) & anti-p14ARF (green). (C) PSN1 xenografts treated with MK-2206 or carrier were stained with DAPI, anti-p53 (DO1) or p53mut (OP29 clone) (D) PSN1 xenografts treated with MK-2206 (60 mg/kg) or carrier were stained by immunohistochemical methods with anti-pS473-AKT, anti-phospho-S48-NPM (pS48-NPM) or p53. (E) PSN1 xenografts established in the flank of athymic nude mice were injected subcutaneously with two alternate day doses of MK-2206 (60 mg/kg) or carrier. Mice were subsequently treated with a single dose of IR (6 Gy) & tumor volumes measured regularly with callipers. Dash lines indicate tumor growth differential at 250 mm3. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25071014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb200-111_rabbit-polyclonal-p14arf-cdkn2a-antibody-310202416203724.jpg)
![Western Blot: p14ARF/CDKN2A Antibody - BSA Free [NB200-111] - Inhibition of AKT decreases p53mut stability(A) T24 cells & PSN1 cells were treated with MK-2206 (5 μM) or DMSO for 24 hrs. Cells were fixed & stained with DAPI & anti-mutant p53 (OP29 clone). (B) T24 cells were pre-treated with MK-2206 (5 μM) or DMSO for 24 hrs before the addition of fresh media containing cyclohexamide (100 μM) (CHX) in combination with MK-2206 (5 μM) or DMSO for the times indicated. Nuclear extracts were prepared from treated cells & blotted with the indicated antibodies. Quantification is relative to initiation of CHX treatment for both conditions *, MK-2206 is 40% of DMSO control but taken as 1.0 for relative assessment. (C) H1299 cells were transfected with HA-tagged-ubiquitin & mutant p53 (R175H or R248W) as indicated. Transfected cells were treated with DMSO, MK-2206 (5 μM) or Nutlin3A (5 μM) for 16hrs as indicated. p53 immunoprecipitates & whole cell lysates were probed with the indicated antibodies. (D) T24 cells were transfected with non-targeting control or p14ARF siRNA & treated with DMSO, MK-2206 (5 μM) or the NPM oligomerisation inhibitor NCS348884 (4 μM) (Qi et al., 2008) as indicated. (E) T24 cells were transfected with non-targeting control, AKT1, or p14ARF siRNA. Cells were treated with NCS348884 (4 μM), Nutlin3A (5 μM) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. (F) KPC mice derived KRASG12D p53 Floxed (p53Fl), KRASG12D p53R172H ARF+/+ & KRASG12D p53R172H ARF−/− pancreatic tumor cells were treated with MK-2206 (1μM), Nutlin3A (5μM) or DMSO as indicated. Whole cell lysates were probed with the indicated antibodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25071014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb200-111_rabbit-polyclonal-p14arf-cdkn2a-antibody-310202416205197.jpg)
![Western Blot: p14ARF/CDKN2A Antibody - BSA Free [NB200-111] - Inhibition of AKT promotes enhanced MDM2 activity via the increased association between NPM & p14ARF(A) Npm−/−, p53−/−double null MEF were infected with pBABE retrovirus empty vector & pBABE expressing FLAG-tagged-NPM-WT, NPM-S48A or S48E as indicated. Immunopurification of NPM was done by pulling down with the Flag tag (middle panel) followed by elution of complexes by the Flag peptide & subsequent immunopurification of endogenous MDM2 (lower panel). (B) Nuclear immunoprecipitates of MDM2 from T24 cells treated with MK-2206 (5 μM, 24 hrs). Immunoprecipitates & lysates were blotted with the indicated antibodies. (C) T24 cells were treated with MK-2206 (5 μM) as indicated. p14ARF was immunoprecipitated from whole cell lysates & nuclear extracts & the association with NPM & MDM2 determined by western blot. Immunoprecipitates & lysates were blotted with the indicated antibodies. (D) MDM2 & (E) p53 ubiquinitation assay in H1299 cells transfected with wild type p53, HA-tagged ubiquitin & treated for 16 hrs with DMSO, MK-2206 (5 μM) or Nutlin3A (5 μM) as indicated. Immunoprecipitates & whole cell lysates were probed with the indicated antibodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25071014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb200-111_rabbit-polyclonal-p14arf-cdkn2a-antibody-310202416212370.jpg)
![Western Blot: p14ARF/CDKN2A Antibody - BSA Free [NB200-111] - Inhibition of AKT promotes enhanced MDM2 activity via the increased association between NPM & p14ARF(A) Npm−/−, p53−/−double null MEF were infected with pBABE retrovirus empty vector & pBABE expressing FLAG-tagged-NPM-WT, NPM-S48A or S48E as indicated. Immunopurification of NPM was done by pulling down with the Flag tag (middle panel) followed by elution of complexes by the Flag peptide & subsequent immunopurification of endogenous MDM2 (lower panel). (B) Nuclear immunoprecipitates of MDM2 from T24 cells treated with MK-2206 (5 μM, 24 hrs). Immunoprecipitates & lysates were blotted with the indicated antibodies. (C) T24 cells were treated with MK-2206 (5 μM) as indicated. p14ARF was immunoprecipitated from whole cell lysates & nuclear extracts & the association with NPM & MDM2 determined by western blot. Immunoprecipitates & lysates were blotted with the indicated antibodies. (D) MDM2 & (E) p53 ubiquinitation assay in H1299 cells transfected with wild type p53, HA-tagged ubiquitin & treated for 16 hrs with DMSO, MK-2206 (5 μM) or Nutlin3A (5 μM) as indicated. Immunoprecipitates & whole cell lysates were probed with the indicated antibodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25071014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb200-111_rabbit-polyclonal-p14arf-cdkn2a-antibody-310202416205120.jpg)
![Western Blot: LC3A Antibody [NBP1-19167] - Total protein from HeLa and Neuro2A cells treated with or without 50 uM chloroquine for 24 hours was separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-LC3A in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Note the detection LC3 II upon chloroquine treatment.](http://images.novusbio.com/fullsize/LC3A-Antibody-Western-Blot-NBP1-19167-img0012.jpg "<b>Biological Strategies Validation. </b>Western Blot: LC3A Antibody [NBP1-19167] - Total protein from HeLa and Neuro2A cells treated with or without 50 uM chloroquine for 24 hours was separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-LC3A in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Note the detection LC3 II upon chloroquine treatment.")
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: LC3A Antibody [NBP1-19167] - LC3/MAP1 [NBP1-19167] - LC3 antibody was tested in HeLa cells with Dylight 488 (green). Cells were treated overnight with 50 uM chloroquine to induce autophagosome formation. Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/LC3A-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-19167-img0013.jpg)
![Immunohistochemistry-Paraffin: LC3A Antibody [NBP1-19167] - Analysis of a FFPE tissue section of mouse brain using LC3 antibody at 1:300 dilution. The signal was developed using HRP-labelled secondary antibody and DAB reagent, and the sections/nuclei were further counterstained with hematoxylin. Note the diffused cytoplasmic staining of LC3 in all of the cells with highest positivity in various neurons.](http://images.novusbio.com/fullsize/LC3A-Antibody-Immunohistochemistry-Paraffin-NBP1-19167-img0014.jpg)
![Western Blot: LC3/MAP1LC3A Antibody [NBP1-19167] - Human brain lysate.](http://images.novusbio.com/fullsize/LC3-MAP1LC3A-Antibody-Western-Blot-NBP1-19167-img0004.jpg)
![Immunohistochemistry-Paraffin: LC3A Antibody [NBP1-19167] - Analysis of a FFPE tissue section of mouse liver using LC3 antibody at 1:300 dilution. The signal was developed using HRP-labelled secondary antibody and DAB reagent, and the sections/nuclei were further counterstained with hematoxylin. Note the diffused cytoplasmic staining of LC3 in all of the hepatocytes and other liver cells.](http://images.novusbio.com/fullsize/LC3-MAP1LC3A-Antibody-Immunohistochemistry-Paraffin-NBP1-19167-img0010.jpg)
![Simple Western: LC3A Antibody [NBP1-19167] - Image shows a specific band for LC3 in 0.5 mg/mL of Neuro2A lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/LC3-MAP1LC3A-Antibody-Simple-Western-NBP1-19167-img0009.jpg)
![Western Blot: DIO3 Antibody [NBP1-05767] - Detection of Dio3 in rat placenta.](http://images.novusbio.com/fullsize/DIO3-Antibody-Western-Blot-NBP1-05767-img0002.jpg "Western Blot: DIO3 Antibody [NBP1-05767] - Detection of Dio3 in rat placenta.")
![Flow Cytometry: DIO3 Antibody [NBP1-05767] - Analysis using the Biotin conjugate of NBP1-05767. Dio3 staining of mouse hepatic stellate cell cultured for 7 days. Image from verified customer review.](http://images.novusbio.com/fullsize/DIO3-Antibody-Flow-Cytometry-NBP1-05767-img0005.jpg)
![Western Blot: DIO3 Antibody [NBP1-05767] - Detection of Dio3 in rabbit brain whole cell homogenate. Photo courtesy of product review by verified customer.](http://images.novusbio.com/fullsize/DIO3-Antibody-Western-Blot-NBP1-05767-img0003.jpg)
