| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2288SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-70207 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-89468-25ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-72627 | |||
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Head and neck cancer cells have different expression levels of the core clock protein BMAL1. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Western-Blot-NB100-2288-img0021.jpg "Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Head and neck cancer cells have different expression levels of the core clock protein BMAL1. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.")
![Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Analysis of BMAL1 in mouse cerebral cortex (left: wt, right: Bmal1 KO) using anti-BMAL1 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Chromatin-Immunoprecipitation-NB100-2288-img0018.jpg)
![<b>Biological Strategies Validation. </b>Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Inhibition of mTOR signaling with Rapamycin rescues PTEN-driven accumulation of BMAL1A. Tissue samples and graphic show BMAL1 in K14cre PtenF/F mice and control (arrows). Note a significant amount of BMAL1 expression in PTEN mutant mice. K14cre PtenF/F mice and control littermates received Rapamycin or vehicle every other day for 15 days. Rapamycin treatment reduces the expression of nuclear BMAL1 in K14cre PtenF/F mice (arrowhead) (*** p0.05). Scale bars -30um. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2288-img0024.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534364.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415171349.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415304255.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241538245.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534379.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534315.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241535633.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1A. Head & neck cancer cells have different expression levels of the core clock protein BMAL1. B. Immunofluorescence assay depicts accumulation of ROS (green channel) & BMAL1 (red channel) upon oxidation. C. & D. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p<0.05, **p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415363747.jpg)
![Immunocytochemistry/ Immunofluorescence: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415523930.jpg)
![Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Astrocyte Bmal1 regulates genes with conflicting effects on A beta deposition. (A) Topro, GFAP, & BMAL1 staining in CA1 hippocampus of 4-month-old BMAL1 aKO; APP/PS1-21 mice & Cre- controls (scale bar = 100 µm). Arrows indicate astrocyte nuclei quantified as indicated by Topro nuclei surrounded by GFAP positivity. Blue circles indicate nuclei quantified as BMAL1 negative. Quantification of astrocytes counted as BMAL1- or BMAL1+ is shown on the right. n = 5 mice per group, **** = p < 0.0001 by two-way ANOVA with Sidak multiple comparisons test. (B) Heatmap of Fluidigm qPCR analysis of 20 genes involved in the circadian clock, glial activation, & Alzheimer’s Disease in cortex from Aldh1l1-CreERT2; Bmal1fl/fl mice & Cre- controls with or without APP/PS1-21 or APPNL-G-F/wt (n = 6–8 mice per group). Two-way ANOVA analysis: c = significant main effect of Cre genotype, m = main effect of A beta model, c*m = interaction effect of cre & A beta model, - = no significance (all p < 0.05). (C) Individually plotted genes from A. * = p < 0.05, ** = p < 0.005, *** = p < 0.0005 by two-way ANOVA with Sidak multiple comparisons test. Panel B was made using GraphPad Prism version 9.2 (//www.graphpad.com). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35110643), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415525251.jpg)
![SDS-Page: Recombinant Human BMAL1 Protein [H00000406-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.](http://images.novusbio.com/fullsize/Recombinant-Human-BMAL1-Protein-SDS-Page-H00000406-P01-img0002.jpg "SDS-Page: Recombinant Human BMAL1 Protein [H00000406-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.")
![Western Blot: NMDAR2A Antibody [NB300-105] - GluN2B to GluN2A NMDAR switch and Ppt1-/--induced synaptic deficits are recapitulated in primary cortical neurons. (B) Representative immunoblot (top) and quantification of GluN2A levels (bottom) in WT and Ppt1-/- neurons at DIV7, 10, and 18. (D) Representative immunoblot (top) and quantification of the GluN2A/2B ratio (bottom) in WT and Ppt1-/- neurons at DIV7, 10, and 18. For all experiments in Figure 5, Ppt1-/- and WT were compared (n = 2 independent experiments with two repetitions/group) at each time point using t-test and the significance indicated as follows: *p<0.05 where indicated. Error bars represent s.e.m. Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/40316) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NMDAR2A-Antibody-Western-Blot-NB300-105-img0006.jpg "Western Blot: NMDAR2A Antibody [NB300-105] - GluN2B to GluN2A NMDAR switch and Ppt1-/--induced synaptic deficits are recapitulated in primary cortical neurons. (B) Representative immunoblot (top) and quantification of GluN2A levels (bottom) in WT and Ppt1-/- neurons at DIV7, 10, and 18. (D) Representative immunoblot (top) and quantification of the GluN2A/2B ratio (bottom) in WT and Ppt1-/- neurons at DIV7, 10, and 18. For all experiments in Figure 5, Ppt1-/- and WT were compared (n = 2 independent experiments with two repetitions/group) at each time point using t-test and the significance indicated as follows: *p<0.05 where indicated. Error bars represent s.e.m. Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/40316) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Western Blot: NMDAR2A Antibody [NB300-105] - Hyperpalmitoylation of Fyn kinase and GluN2B is reversed in Ppt1-/- primary cortical neurons by palmitoylation inhibitor treatment. Representative post-APEGS immunoblot of GluN2A (NMDAR2A) with beta-actin loading control. Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/40316), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NMDAR2A-Antibody-Western-Blot-NB300-105-img0007.jpg)
![Immunohistochemistry: NMDAR2A Antibody [NB300-105] - Immunostaining of rabbit retina showing NR2A in the rod and cone photoreceptors in the outer plexiform layer as well as the entire inner plexiform layer.](http://images.novusbio.com/fullsize/NMDAR2A-Antibody-Immunohistochemistry-NB300-105-img0004.jpg)
![Western Blot: NMDAR2A Antibody [NB300-105]](http://images.novusbio.com/fullsize/NMDAR2A-Antibody-Western-Blot-NB300-105-img0005.jpg)
![Western Blot: NMDAR2A Antibody [NB300-105] - NMDAR subunit composition is immature in whole lysates from Ppt1-/- visual cortex.(A) Representative immunoblots of the GluN2A in whole lysates across age & genotype as indicated (top) & quantification of band density (bottom) normalized to beta -actin loading control within lane. (B) Representative immunoblots of the GluN2B in whole lysates across age & genotype as indicated (top) & quantification of band density (bottom) normalized to beta -actin loading control within lane. (C) Representative immunoblots of GluN2A & GluN2B (top) from whole lysates across age & genotype & quantification of the ratio of GluN2A/GluN2B band density within animal (bottom). (D) Representative immunoblots of GluN1 in whole lysates across age & genotype as indicated (top) & quantification of band density (bottom) normalized to beta -actin loading control within lane. (E) Representative immunoblot from whole lysates of PPT1 across age & genotype as indicated (top) & protein expression level (bottom) normalized to beta -actin. For experiments in Figure 2—figure supplement 1A–C, Ppt1-/- & WT were compared (n = 4 independent experiments/animals with two repetitions/group) at each age using t-test & the significance is indicated: *p<0.05. In Figure 2D, WT expression levels at each age were compared (n = 4 independent experiments/animals with two repetitions/group) by ANOVA followed by Tukey’s post-hoc test. Significance between ages is indicated: *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001. Error bars represent s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30946007), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-105_rabbit-polyclonal-nmdar2a-antibody-310202416203711.jpg)
![Western Blot: NMDAR2A Antibody [NB300-105] - GluN2B to GluN2A NMDAR switch & Ppt1-/--induced synaptic deficits are recapitulated in primary cortical neurons.(A) Representative immunoblot (top) & quantification of GluN2B levels in WT & Ppt1-/- neurons at DIV7, 10, & 18. (B) Representative immunoblot (top) & quantification of GluN2A levels (bottom) in WT & Ppt1-/- neurons at DIV7, 10, & 18. (C) Representative immunoblot (top) & quantification of PSD-95 levels (bottom) in WT & Ppt1-/- neurons at DIV7, 10, & 18. (D) Representative immunoblot (top) & quantification of the GluN2A/2B ratio (bottom) in WT & Ppt1-/- neurons at DIV7, 10, & 18. For all experiments in Figure 5, Ppt1-/- & WT were compared (n = 2 independent experiments with two repetitions/group) at each time point using t-test & the significance indicated as follows: *p<0.05 where indicated. Error bars represent s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30946007), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-105_rabbit-polyclonal-nmdar2a-antibody-31020241620374.jpg)
![Western Blot: NMDAR2A Antibody [NB300-105] - NMDAR subunit composition is immature in whole lysates from Ppt1-/- visual cortex.(A) Representative immunoblots of the GluN2A in whole lysates across age & genotype as indicated (top) & quantification of band density (bottom) normalized to beta -actin loading control within lane. (B) Representative immunoblots of the GluN2B in whole lysates across age & genotype as indicated (top) & quantification of band density (bottom) normalized to beta -actin loading control within lane. (C) Representative immunoblots of GluN2A & GluN2B (top) from whole lysates across age & genotype & quantification of the ratio of GluN2A/GluN2B band density within animal (bottom). (D) Representative immunoblots of GluN1 in whole lysates across age & genotype as indicated (top) & quantification of band density (bottom) normalized to beta -actin loading control within lane. (E) Representative immunoblot from whole lysates of PPT1 across age & genotype as indicated (top) & protein expression level (bottom) normalized to beta -actin. For experiments in Figure 2—figure supplement 1A–C, Ppt1-/- & WT were compared (n = 4 independent experiments/animals with two repetitions/group) at each age using t-test & the significance is indicated: *p<0.05. In Figure 2D, WT expression levels at each age were compared (n = 4 independent experiments/animals with two repetitions/group) by ANOVA followed by Tukey’s post-hoc test. Significance between ages is indicated: *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001. Error bars represent s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30946007), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-105_rabbit-polyclonal-nmdar2a-antibody-310202416205181.jpg)
![Western Blot: NMDAR2A Antibody [NB300-105] - GluN2B to GluN2A NMDAR switch & Ppt1-/--induced synaptic deficits are recapitulated in primary cortical neurons.(A) Representative immunoblot (top) & quantification of GluN2B levels in WT & Ppt1-/- neurons at DIV7, 10, & 18. (B) Representative immunoblot (top) & quantification of GluN2A levels (bottom) in WT & Ppt1-/- neurons at DIV7, 10, & 18. (C) Representative immunoblot (top) & quantification of PSD-95 levels (bottom) in WT & Ppt1-/- neurons at DIV7, 10, & 18. (D) Representative immunoblot (top) & quantification of the GluN2A/2B ratio (bottom) in WT & Ppt1-/- neurons at DIV7, 10, & 18. For all experiments in Figure 5, Ppt1-/- & WT were compared (n = 2 independent experiments with two repetitions/group) at each time point using t-test & the significance indicated as follows: *p<0.05 where indicated. Error bars represent s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30946007), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-105_rabbit-polyclonal-nmdar2a-antibody-310202416212371.jpg)
![Western Blot: NMDAR2B Antibody [NB300-106] - The blots show the examples of immunobands against NMDAR2B (C) and beta-actin antibodies on the membrane, which was performed on the membrane protein prepared from the lumbar spinal cords of the offspring (P14) rats in different groups. Image collected and cropped by CiteAb from the following publication (//www.jbiomedsci.com/content/18/1/64) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NMDAR2B-Antibody-Western-Blot-NB300-106-img0006.jpg "Western Blot: NMDAR2B Antibody [NB300-106] - The blots show the examples of immunobands against NMDAR2B (C) and beta-actin antibodies on the membrane, which was performed on the membrane protein prepared from the lumbar spinal cords of the offspring (P14) rats in different groups. Image collected and cropped by CiteAb from the following publication (//www.jbiomedsci.com/content/18/1/64) licensed under a CC-BY license.")
![Flow Cytometry: NMDAR2B Antibody [NB300-106] - NMDA2B receptor expression on CD4+ T cells. Image supplied by review from confirmed customer.](http://images.novusbio.com/fullsize/NMDAR2B-Antibody-Flow-Cytometry-NB300-106-img0004.jpg)
![Western Blot: NMDAR2B Antibody [NB300-106]](http://images.novusbio.com/fullsize/NMDAR2B-Antibody-Western-Blot-NB300-106-img0005.jpg)
![Western Blot: GPER/GPR30 Antibody [NBP1-31239] - The MW of GPR30 is estimated to be 42 kDa, but higher MW sizes have been reported due to glycosylation and interaction with other proteins. Bands are identified as glycosylated and nonglycosylated based on reports cited in the text, but could include interaction with other proteins. For each GPER western, the membrane was stripped and reprobed for b-actin as a loading control. Quantitation of GPER was evaluated by summing all immunoreactive bands and dividing by b-actin, then normalizing to HBEC2-KT in each blot. Image collected and cropped by CiteAb from the following publication (biomedcentral.com/1471-2407/12/624), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Western-Blot-NBP1-31239-img0012.jpg "Western Blot: GPER/GPR30 Antibody [NBP1-31239] - The MW of GPR30 is estimated to be 42 kDa, but higher MW sizes have been reported due to glycosylation and interaction with other proteins. Bands are identified as glycosylated and nonglycosylated based on reports cited in the text, but could include interaction with other proteins. For each GPER western, the membrane was stripped and reprobed for b-actin as a loading control. Quantitation of GPER was evaluated by summing all immunoreactive bands and dividing by b-actin, then normalizing to HBEC2-KT in each blot. Image collected and cropped by CiteAb from the following publication (biomedcentral.com/1471-2407/12/624), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: GPER/GPR30 Antibody [NBP1-31239] - Detection of GPER/GPR30 in HUVEC nucleus. Image courtesy of a product review by Dr. Subhadeep Chakrabarti of University of Alberta.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-31239-img0010.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: GPER/GPR30 Antibody [NBP1-31239] - A. 50 ug 293T whole cell lysate/extract. B. 50 ug whole cell lysate/extract of GFP-human GPR30-transfected 293T cells (No boiling). C. 50 ug whole cell lysate/extract of GFP-human GPR30 and GPR30 siRNA-transfected 293T cells (No boiling). 5 % SDS-PAGE GPR30 antibody ) dilution: 1:1000](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Western-Blot-NBP1-31239-img0011.jpg)
![Western Blot: GPER/GPR30 Antibody [NBP1-31239] - AhR & GPR30 receptors are present & functional in the MCF10AT1 cells. (A) RT-qPCR analysis of AhR & GPR30 mRNA expression levels represented in arbitrary units (a.u.) in the MCF10AT1 & MCF10CA1a.cl1 cells. MCF-7 cells were used as a control. Values represent mean ± SD of three independent experiments conducted in triplicate. (B) Representative Western blot analyses from three independent experiments of AhR & GPR30 protein expression in MCF10AT1 & MCF10CA1a.cl1 cells. MCF-7 cells were used as a control. (C) XRE-luciferase activity following 8 h exposure of MCF10AT1 cells to ITE at the indicated concentrations. TCDD 10−7 M was used as a control & results were expressed as % of TCDD 10−7 M activity. ***p < 0.001 in Student t-test. (D) XRE-luciferase activity upon 8 h of exposure to ITE 10−10 M alone or in combination with GNF351 at the indicated concentrations. TCDD 10−7 M was used as a control, & results were expressed as % of TCDD 10−7 M activity. Student t-tests revealed the statistically significant differences between unexposed & exposed cells: ***p < 0.001; & between ITE & ITE+GNF351: ###p < 0.001. Values in (C,D) represent mean ± SD of three independent experiments. (E) Representative Western blot analyses from three independent experiments of the phospho-MAPK/MAPK ratio upon exposure of MCF10AT1 cells to G1 (GPR30 agonist) for the times indicated, in the presence or absence of a 2 h pre-treatment with G15 (GPR30 antagonist). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32670863), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-31239_rabbit-polyclonal-gper-gpr30-antibody-310202416171440.jpg)
![Western Blot: GPER/GPR30 Antibody [NBP1-31239] - Effects of short-term exposure of BPA, B[a]P, ITE & G1 10−10 M on AIG & MFE are inhibited by siRNA-AhR & siRNA-GPR30. Representative Western blot analysis from three independent experiments of AhR & GPR30 expression in transfected MCF10AT1 cells with (A) siRNA-AhR, (B) siRNA-GPR30 or their scrambled controls. Quantification of protein expression levels was normalized against tubulin expression. (C,D) Secondary mammospheres formation & (E,F) average number of colonies in soft agar, with the following treatments: BPA and/or B[a]P, G1, or ITE, 10−10 M. Cells were transfected with either siRNA-AhR, siRNA-GPR30 or their scrambled controls before being subjected to the treatments. Treatments were maintained throughout the course of experiments. (mean ± SD of 2 independent experiments, in triplicate). ***p < 0.001, *p < 0.05 vs. their respective unexposed; ###p < 0.001 siRNA vs. scrambled in Student t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32670863), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-31239_rabbit-polyclonal-gper-gpr30-antibody-310202416173515.jpg)
![Western Blot: GPER/GPR30 Antibody [NBP1-31239] - Human endothelial cells express GPR30 protein in the cell nucleus.(A) Confluent monolayers of HUVECs from 3 different cords were lysed & the protein lysates were immunoblotted for GPR30. alpha -tubulin was used as loading control. (B) HUVEC monolayers at 30–40% confluence were treated with 40 nM siRNA (control or GPR30_4) for 48 hours prior to lysis followed by immunoblotting of the cell lysates for GPR30. alpha -tubulin was used as loading control. Data shown are mean ± SEM of 4 independent experiments. ** & ## indicate p<0.01 compared to untreated & control siRNA-treated cells, respectively. (C) Confluent HUVECs grown on glass coverslips were fixed, permeabilized & immunostained with anti-GPR30 antibody. Nuclei were stained with Hoechst33342 dye. The merged image shows GPR30 (red) & nuclei (blue) in pseudocolor. Representative images from 3 independent experiments are shown. Bar, 20 µm. (D) Confluent HUVECs were lysed & fractionated into cytosolic (C) & nuclear (N) fractions prior to western blotting for eNOS, GPR30, p65, alpha -tubulin & c-Jun. A representative set of images (obtained from different membranes) from 3 independent experiments is shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23285008), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-31239_rabbit-polyclonal-gper-gpr30-antibody-310202416175294.jpg)
![Western Blot: GPER/GPR30 Antibody [NBP1-31239] - Effects of short-term exposure of BPA, B[a]P, ITE & G1 10−10 M on AIG & MFE are inhibited by siRNA-AhR & siRNA-GPR30. Representative Western blot analysis from three independent experiments of AhR & GPR30 expression in transfected MCF10AT1 cells with (A) siRNA-AhR, (B) siRNA-GPR30 or their scrambled controls. Quantification of protein expression levels was normalized against tubulin expression. (C,D) Secondary mammospheres formation & (E,F) average number of colonies in soft agar, with the following treatments: BPA and/or B[a]P, G1, or ITE, 10−10 M. Cells were transfected with either siRNA-AhR, siRNA-GPR30 or their scrambled controls before being subjected to the treatments. Treatments were maintained throughout the course of experiments. (mean ± SD of 2 independent experiments, in triplicate). ***p < 0.001, *p < 0.05 vs. their respective unexposed; ###p < 0.001 siRNA vs. scrambled in Student t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32670863), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-31239_rabbit-polyclonal-gper-gpr30-antibody-310202416173516.jpg)
![Western Blot: GPER/GPR30 Antibody [NBP1-31239] - Effects of short-term exposure of BPA, B[a]P, ITE & G1 10−10 M on AIG & MFE are inhibited by siRNA-AhR & siRNA-GPR30. Representative Western blot analysis from three independent experiments of AhR & GPR30 expression in transfected MCF10AT1 cells with (A) siRNA-AhR, (B) siRNA-GPR30 or their scrambled controls. Quantification of protein expression levels was normalized against tubulin expression. (C,D) Secondary mammospheres formation & (E,F) average number of colonies in soft agar, with the following treatments: BPA and/or B[a]P, G1, or ITE, 10−10 M. Cells were transfected with either siRNA-AhR, siRNA-GPR30 or their scrambled controls before being subjected to the treatments. Treatments were maintained throughout the course of experiments. (mean ± SD of 2 independent experiments, in triplicate). ***p < 0.001, *p < 0.05 vs. their respective unexposed; ###p < 0.001 siRNA vs. scrambled in Student t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32670863), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-31239_rabbit-polyclonal-gper-gpr30-antibody-310202416163721.jpg)
![Western Blot: BMAL1 Antibody (OTI1C11) [NBP2-02544] - HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY BMAL1 (Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-BMAL1.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Western-Blot-NBP2-02544-img0013.jpg "Western Blot: BMAL1 Antibody (OTI1C11) [NBP2-02544] - HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY BMAL1 (Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-BMAL1.")
![Immunocytochemistry/Immunofluorescence: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of COS7 cells transiently transfected by pCMV6-ENTRY ARNTL .](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunocytochemistry-Immunofluorescence-NBP2-02544-img0014.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded Carcinoma of prostate tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0012.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded Adenocarcinoma of ovary tissue N93ing anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0003.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded colon tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0006.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded lung tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0007.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded pancreas tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0008.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded prostate tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0009.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded Adenocarcinoma of colon tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0010.jpg)
![Immunohistochemistry-Paraffin: BMAL1 Antibody (OTI1C11) [NBP2-02544] - Staining of paraffin-embedded bladder tissue using anti-BMAL1 mouse monoclonal antibody.](http://images.novusbio.com/fullsize/BMAL1-Antibody-OTI1C11-Immunohistochemistry-Paraffin-NBP2-02544-img0011.jpg)
![Western Blot: SIN3A Antibody [NB600-1263] - Analysis of K562 cell extract.](http://images.novusbio.com/fullsize/SIN3A-Antibody-Western-Blot-NB600-1263-img0003.jpg "Western Blot: SIN3A Antibody [NB600-1263] - Analysis of K562 cell extract.")
![Immunocytochemistry/Immunofluorescence: SIN3A Antibody [NB600-1263] - Analysis of Sin3A (green) showing staining in the nucleus of A431 cells (right) compared to a negative control without primary antibody (left).](http://images.novusbio.com/fullsize/SIN3A-Antibody-Immunocytochemistry-Immunofluorescence-NB600-1263-img0008.jpg)
![Immunohistochemistry-Paraffin: SIN3A Antibody [NB600-1263] - Analysis showing staining in the nucleus of human ovary carcinoma (right) compared to a negative control without primary antibody (left).](http://images.novusbio.com/fullsize/SIN3A-Antibody-Immunohistochemistry-Paraffin-NB600-1263-img0009.jpg)
![Chromatin Immunoprecipitation: SIN3A Antibody [NB600-1263] - Analysis of Sin3A performed using cross-linked chromatin from colon carcinoma cells treated with serum. Immunoprecipitation performed using a multiplex microplate Matrix ChIP assay with Sin3A polyclonal antibody. Chromatin aliquots from cells were used per ChIP pull-down. Quantitative PCR data done in quadruplicate using 1ul of eluted DNA in 2ul SYBR real-time PCR reactions containing primers to amplify -15kb upstream of the Egr1 gene or exon-1 or exon-2 of Egr1. Quantitation of immunoprecipitated chromatin is presented as signal relative to the total amount of input chromatin. A representation of the Egr-1 locus is shown; boxes represent exons (black boxes = translated, white boxes = untranslated), the zigzag line represents an intron, and the straight line represents upstream sequence. Regions amplified by Egr-1 primers are represented by black bars. Data courtesy of the Innovators Program.](http://images.novusbio.com/fullsize/SIN3A-Antibody-Chromatin-Immunoprecipitation-ChIP-NB600-1263-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: SIN3A Antibody [NB600-1263] - Analysis of Sin3A (green) showing staining in the nucleus of NIH-3T3 cells (right) compared to a negative control without primary antibody (left).](http://images.novusbio.com/fullsize/SIN3A-Antibody-Immunocytochemistry-Immunofluorescence-NB600-1263-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: SIN3A Antibody [NB600-1263] - Analysis of Sin3A (green) showing staining in the nucleus of Hela cells (right) compared to a negative control without primary antibody (left).](http://images.novusbio.com/fullsize/SIN3A-Antibody-Immunocytochemistry-Immunofluorescence-NB600-1263-img0007.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Human breast carcinoma.Tissue after heat-induced antigen retrieval.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0010.jpg "Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Human breast carcinoma.Tissue after heat-induced antigen retrieval.")
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Analysis of anti-GPER1 / GPR30 antibody with breast carcinoma.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0001.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Analysis of anti-GPER1 / GPR30 antibody with human, pancreas, islet.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0003.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Analysis of anti-GPER1 / GPR30 antibody with human adrenal.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0004.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Human Skin, Melanoma formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0005.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Anti-GPER1 / GPR30 antibody IHC of human colon, carcinoma. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0006.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Anti-GPER1 / GPR30 antibody IHC of human Lung, Small Cell Carcinoma. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval.](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0007.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Brain, Parkinson's Lewy Body](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0008.jpg)
![Immunohistochemistry-Paraffin: GPER/GPR30 Antibody [NLS1183] - Brain, cerebellum, Purkinje neuron](http://images.novusbio.com/fullsize/GPER-GPR30-Antibody-Immunohistochemistry-Paraffin-NLS1183-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: MEF2C Antibody [NBP1-89468] - Staining of human cell line RH-30 shows localization to nucleoplasm & vesicles. Antibody staining is shown in green.](http://images.novusbio.com/fullsize/MEF2C-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-89468-img0003.jpg "Immunocytochemistry/Immunofluorescence: MEF2C Antibody [NBP1-89468] - Staining of human cell line RH-30 shows localization to nucleoplasm & vesicles. Antibody staining is shown in green.")
![Western Blot: Brg1 Antibody [NB100-2594] - Whole cell lysate (15 ug) from HeLa, HEK293T, and Jurkat cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-BRG1/SMARCA4 antibodyused for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 30seconds.](http://images.novusbio.com/fullsize/Brg1-Antibody-Western-Blot-NB100-2594-img0019.jpg "Western Blot: Brg1 Antibody [NB100-2594] - Whole cell lysate (15 ug) from HeLa, HEK293T, and Jurkat cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-BRG1/SMARCA4 antibodyused for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 30seconds.")
![Immunohistochemistry-Paraffin: Brg1 Antibody [NB100-2594] - Section of human ovarian carcinoma. Antibody: Affinity purified rabbit antiBRG1/SMARCA4 used at a dilution of 1:1,000 (0.2ug/ml). Detection: DAB](http://images.novusbio.com/fullsize/Brg1-Antibody-Immunohistochemistry-Paraffin-NB100-2594-img0017.jpg)
![Western Blot: Brg1 Antibody [NB100-2594] - Whole cell lysate (15 ug) from NIH 3T3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-BRG1/SMARCA4 antibody used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes.](http://images.novusbio.com/fullsize/Brg1-Antibody-Western-Blot-NB100-2594-img0018.jpg)
![Immunohistochemistry-Paraffin: Brg1 Antibody [NB100-2594] - Section of mouse renal cell carcinoma. Antibody: Affinity purified rabbit antiBRG1/SMARCA4 used at a dilution of 1:1,000 (0.2ug/ml). Detection: DAB](http://images.novusbio.com/fullsize/Brg1-Antibody-Immunohistochemistry-Paraffin-NB100-2594-img0016.jpg)
![<b>Independent Antibodies Validation. </b>Immunoprecipitation: Brg1 Antibody [NB100-2594] - Detection of human BRG1-SMARCA4 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-BRG1-SMARCA4 antibody NB100-2594 used for IP at 3 ug per reaction. BRG1-SMARCA4 was also immunoprecipitated by rabbit anti-BRG1-SMARCA4 antibody NBP-22234. For blotting immunoprecipitated BRG1-SMARCA4, NB100-2594 was used at 1 ug/ml. Detection: Chemiluminescence with an exposure time of 30 seconds.](http://images.novusbio.com/fullsize/Brg1-Antibody-Immunoprecipitation-NB100-2594-img0020.jpg)
![Western Blot: MEF2C Antibody (1H5) [NBP2-00493] - HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY MEF2C (Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-MEF2C.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Western-Blot-NBP2-00493-img0004.jpg "Western Blot: MEF2C Antibody (1H5) [NBP2-00493] - HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY MEF2C (Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-MEF2C.")
![Immunocytochemistry/Immunofluorescence: MEF2C Antibody (OTI1H5) [NBP2-00493] - MEF2C Antibody (1H5) [NBP2-00493] - Staining of COS7 cells transiently transfected by pCMV6-ENTRY MEF2C.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Immunocytochemistry-Immunofluorescence-NBP2-00493-img0010.jpg)
![Immunohistochemistry-Paraffin: MEF2C Antibody (1H5) [NBP2-00493] - Staining of paraffin-embedded Human Ovary tissue using anti-MEF2C mouse monoclonal antibody.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Immunohistochemistry-Paraffin-NBP2-00493-img0008.jpg)
![Flow Cytometry: MEF2C Antibody (1H5) [NBP2-00493] - HEK293T cells transfected with either overexpression plasmid (Red) or empty vector control plasmid (Blue) were immunostained by anti-MEF2C antibody, and then analyzed by flow cytometry.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Flow-Cytometry-NBP2-00493-img0003.jpg)
![Immunohistochemistry-Paraffin: MEF2C Antibody (1H5) [NBP2-00493] - Staining of paraffin-embedded Carcinoma of Human prostate tissue using anti-MEF2C mouse monoclonal antibody.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Immunohistochemistry-Paraffin-NBP2-00493-img0005.jpg)
![Immunohistochemistry-Paraffin: MEF2C Antibody (1H5) [NBP2-00493] - Staining of paraffin-embedded Human lymph node tissue using anti-MEF2C mouse monoclonal antibody.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Immunohistochemistry-Paraffin-NBP2-00493-img0006.jpg)
![Immunohistochemistry-Paraffin: MEF2C Antibody (1H5) [NBP2-00493] - Staining of paraffin-embedded Human lymphoma tissue using anti-MEF2C mouse monoclonal antibody.](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Immunohistochemistry-Paraffin-NBP2-00493-img0007.jpg)
![Flow Cytometry: MEF2C Antibody (1H5) [NBP2-00493] - Analysis of Hela cells, using anti-MEF2C antibody, (Red), compared to a nonspecific negative control antibody (Blue).](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Flow-Cytometry-NBP2-00493-img0001.jpg)
![Flow Cytometry: MEF2C Antibody (1H5) [NBP2-00493] - Analysis of Jurkat cells, using anti-MEF2C antibody, (Red), compared to a nonspecific negative control antibody (Blue).](http://images.novusbio.com/fullsize/MEF2C-Antibody-1H5-Flow-Cytometry-NBP2-00493-img0002.jpg)
![Immunohistochemistry-Paraffin: MEF2C Antibody [NBP2-17260] - Mouse brain. MEF2C stained by MEF2C antibody diluted at 1:250. Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.](http://images.novusbio.com/fullsize/MEF2C-Antibody-Immunohistochemistry-Paraffin-NBP2-17260-img0018.jpg "Immunohistochemistry-Paraffin: MEF2C Antibody [NBP2-17260] - Mouse brain. MEF2C stained by MEF2C antibody diluted at 1:250. Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.")
![Immunohistochemistry-Paraffin: MEF2C Antibody [NBP2-17260] - Mouse fore brain. MEF2C antibody dilution: 1:500. Antigen Retrieval: Trilogy™ (EDTA based, pH 8.0) buffer, 15min.](http://images.novusbio.com/fullsize/MEF2C-Antibody-Immunohistochemistry-NBP2-17260-img0005.jpg)
![Immunohistochemistry-Paraffin: MEF2C Antibody [NBP2-17260] - Saos2 xenograft. MEF2C antibody dilution: 1:500. Antigen Retrieval: Trilogy™ (EDTA based, pH 8.0) buffer, 15min.](http://images.novusbio.com/fullsize/MEF2C-Antibody-Immunohistochemistry-Paraffin-NBP2-17260-img0007.jpg)
![Western Blot: MEF2C Antibody [NBP2-17260] - Various whole cell extracts (30 ug) were separated by 10% SDS-PAGE, and the membrane was blotted with MEF2C antibody (NBP2-17260) diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nbp2-17260_rabbit-polyclonal-mef2c-antibody-910202420131220.jpg)
![MEF2C antibody immunoprecipitates MEF2C protein in IP experiments.IP samples: K562 whole cell extractA. Control with 4 ug of preimmune Rabbit IgGB. Immunoprecipitation of MEF2C protein by 4 ug MEF2C antibody (NBP2-17260)5 % SDS-PAGEThe immunoprecipitated MEF2C protein was detected by MEF2C antibody (NBP2-17260) diluted at 1:1000.[EasyBlot anti-rabbit IgG was used as a secondary reagent]](http://images.novusbio.com/fullsize/nbp2-17260_rabbit-polyclonal-mef2c-antibody-immunoprecipitation-261120251821333.jpg)
