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anti ezh2 antibodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ezh2 antibodies
    Anti Ezh2 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1414 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti ezh2 antibodies/product/Cell Signaling Technology Inc
    Average 98 stars, based on 1414 article reviews
    anti ezh2 antibodies - by Bioz Stars, 2026-02
    98/100 stars

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    a + b Control and IκBζ-overexpressing B16-F10 cells were treated for 24 h with 1.5 µM RGFP966 (HDAC3i) or 5 µM Tazemetostat (EZH2i). a Relative gene expression was normalized to Actb . b Immunoblot analysis of IκBζ overexpression and inhibitor controls for HDAC3 inhibition (Ac-H3) and <t>EZH2</t> inhibition (H3K27me3). β-Actin served as a loading control. c Co-immunoprecipitation (IP) of human IκBζ in control and IκBζ-overexpressing B16-F10 cells. Immunoblot detection was performed using an HDAC3 or EZH2 antibody. IκBζ detection served as a positive control for the co-immunoprecipitation. β-Actin was used as a loading control for the input. d Left: Chromatin immunoprecipitation (ChIP) assays of IgG (as control) and HDAC3 in control and IκBζ-overexpressing B16-F10 cells. Right: ChIP assays of H3K27me3 and H3 in control and IκBζ-overexpressing B16-F10 cells. Actb served as a negative control for the H3K27me3 ChIP. e ChIP assays of IgG (as control) and HDAC3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. Right: ChIP assays of H3K27me3 and H3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. RPL37A served as a negative control for the H3K27me3 ChIP. Data derive from 3 independent experiments (mean ± standard deviation ( SD )). Significance was calculated using a two-tailed Student’s t-test (* p < 0.05, ** p < 0.01, and *** p < 0.001, ns = not significant). Source data and exact P values are provided in the Source Data file.
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    a + b Control and IκBζ-overexpressing B16-F10 cells were treated for 24 h with 1.5 µM RGFP966 (HDAC3i) or 5 µM Tazemetostat (EZH2i). a Relative gene expression was normalized to Actb . b Immunoblot analysis of IκBζ overexpression and inhibitor controls for HDAC3 inhibition (Ac-H3) and <t>EZH2</t> inhibition (H3K27me3). β-Actin served as a loading control. c Co-immunoprecipitation (IP) of human IκBζ in control and IκBζ-overexpressing B16-F10 cells. Immunoblot detection was performed using an HDAC3 or EZH2 antibody. IκBζ detection served as a positive control for the co-immunoprecipitation. β-Actin was used as a loading control for the input. d Left: Chromatin immunoprecipitation (ChIP) assays of IgG (as control) and HDAC3 in control and IκBζ-overexpressing B16-F10 cells. Right: ChIP assays of H3K27me3 and H3 in control and IκBζ-overexpressing B16-F10 cells. Actb served as a negative control for the H3K27me3 ChIP. e ChIP assays of IgG (as control) and HDAC3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. Right: ChIP assays of H3K27me3 and H3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. RPL37A served as a negative control for the H3K27me3 ChIP. Data derive from 3 independent experiments (mean ± standard deviation ( SD )). Significance was calculated using a two-tailed Student’s t-test (* p < 0.05, ** p < 0.01, and *** p < 0.001, ns = not significant). Source data and exact P values are provided in the Source Data file.
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    a + b Control and IκBζ-overexpressing B16-F10 cells were treated for 24 h with 1.5 µM RGFP966 (HDAC3i) or 5 µM Tazemetostat (EZH2i). a Relative gene expression was normalized to Actb . b Immunoblot analysis of IκBζ overexpression and inhibitor controls for HDAC3 inhibition (Ac-H3) and <t>EZH2</t> inhibition (H3K27me3). β-Actin served as a loading control. c Co-immunoprecipitation (IP) of human IκBζ in control and IκBζ-overexpressing B16-F10 cells. Immunoblot detection was performed using an HDAC3 or EZH2 antibody. IκBζ detection served as a positive control for the co-immunoprecipitation. β-Actin was used as a loading control for the input. d Left: Chromatin immunoprecipitation (ChIP) assays of IgG (as control) and HDAC3 in control and IκBζ-overexpressing B16-F10 cells. Right: ChIP assays of H3K27me3 and H3 in control and IκBζ-overexpressing B16-F10 cells. Actb served as a negative control for the H3K27me3 ChIP. e ChIP assays of IgG (as control) and HDAC3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. Right: ChIP assays of H3K27me3 and H3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. RPL37A served as a negative control for the H3K27me3 ChIP. Data derive from 3 independent experiments (mean ± standard deviation ( SD )). Significance was calculated using a two-tailed Student’s t-test (* p < 0.05, ** p < 0.01, and *** p < 0.001, ns = not significant). Source data and exact P values are provided in the Source Data file.
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    a + b Control and IκBζ-overexpressing B16-F10 cells were treated for 24 h with 1.5 µM RGFP966 (HDAC3i) or 5 µM Tazemetostat (EZH2i). a Relative gene expression was normalized to Actb . b Immunoblot analysis of IκBζ overexpression and inhibitor controls for HDAC3 inhibition (Ac-H3) and <t>EZH2</t> inhibition (H3K27me3). β-Actin served as a loading control. c Co-immunoprecipitation (IP) of human IκBζ in control and IκBζ-overexpressing B16-F10 cells. Immunoblot detection was performed using an HDAC3 or EZH2 antibody. IκBζ detection served as a positive control for the co-immunoprecipitation. β-Actin was used as a loading control for the input. d Left: Chromatin immunoprecipitation (ChIP) assays of IgG (as control) and HDAC3 in control and IκBζ-overexpressing B16-F10 cells. Right: ChIP assays of H3K27me3 and H3 in control and IκBζ-overexpressing B16-F10 cells. Actb served as a negative control for the H3K27me3 ChIP. e ChIP assays of IgG (as control) and HDAC3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. Right: ChIP assays of H3K27me3 and H3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. RPL37A served as a negative control for the H3K27me3 ChIP. Data derive from 3 independent experiments (mean ± standard deviation ( SD )). Significance was calculated using a two-tailed Student’s t-test (* p < 0.05, ** p < 0.01, and *** p < 0.001, ns = not significant). Source data and exact P values are provided in the Source Data file.
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    a + b Control and IκBζ-overexpressing B16-F10 cells were treated for 24 h with 1.5 µM RGFP966 (HDAC3i) or 5 µM Tazemetostat (EZH2i). a Relative gene expression was normalized to Actb . b Immunoblot analysis of IκBζ overexpression and inhibitor controls for HDAC3 inhibition (Ac-H3) and EZH2 inhibition (H3K27me3). β-Actin served as a loading control. c Co-immunoprecipitation (IP) of human IκBζ in control and IκBζ-overexpressing B16-F10 cells. Immunoblot detection was performed using an HDAC3 or EZH2 antibody. IκBζ detection served as a positive control for the co-immunoprecipitation. β-Actin was used as a loading control for the input. d Left: Chromatin immunoprecipitation (ChIP) assays of IgG (as control) and HDAC3 in control and IκBζ-overexpressing B16-F10 cells. Right: ChIP assays of H3K27me3 and H3 in control and IκBζ-overexpressing B16-F10 cells. Actb served as a negative control for the H3K27me3 ChIP. e ChIP assays of IgG (as control) and HDAC3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. Right: ChIP assays of H3K27me3 and H3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. RPL37A served as a negative control for the H3K27me3 ChIP. Data derive from 3 independent experiments (mean ± standard deviation ( SD )). Significance was calculated using a two-tailed Student’s t-test (* p < 0.05, ** p < 0.01, and *** p < 0.001, ns = not significant). Source data and exact P values are provided in the Source Data file.

    Journal: Nature Communications

    Article Title: Constitutive expression of the transcriptional co-activator IκBζ promotes melanoma growth and immunotherapy resistance

    doi: 10.1038/s41467-025-60929-5

    Figure Lengend Snippet: a + b Control and IκBζ-overexpressing B16-F10 cells were treated for 24 h with 1.5 µM RGFP966 (HDAC3i) or 5 µM Tazemetostat (EZH2i). a Relative gene expression was normalized to Actb . b Immunoblot analysis of IκBζ overexpression and inhibitor controls for HDAC3 inhibition (Ac-H3) and EZH2 inhibition (H3K27me3). β-Actin served as a loading control. c Co-immunoprecipitation (IP) of human IκBζ in control and IκBζ-overexpressing B16-F10 cells. Immunoblot detection was performed using an HDAC3 or EZH2 antibody. IκBζ detection served as a positive control for the co-immunoprecipitation. β-Actin was used as a loading control for the input. d Left: Chromatin immunoprecipitation (ChIP) assays of IgG (as control) and HDAC3 in control and IκBζ-overexpressing B16-F10 cells. Right: ChIP assays of H3K27me3 and H3 in control and IκBζ-overexpressing B16-F10 cells. Actb served as a negative control for the H3K27me3 ChIP. e ChIP assays of IgG (as control) and HDAC3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. Right: ChIP assays of H3K27me3 and H3 in shRNA control and NFKBIZ knockdown LOX-IMVI cells. RPL37A served as a negative control for the H3K27me3 ChIP. Data derive from 3 independent experiments (mean ± standard deviation ( SD )). Significance was calculated using a two-tailed Student’s t-test (* p < 0.05, ** p < 0.01, and *** p < 0.001, ns = not significant). Source data and exact P values are provided in the Source Data file.

    Article Snippet: Pulldown samples were analyzed by SDS-PAGE and detected by immunoblotting using a FLAG antibody (Sigma, Cat. F1804), HDAC3 (Cell Signaling, Cat. 85057), or EZH2 antibody (Cell Signaling, Cat. 5246).

    Techniques: Control, Gene Expression, Western Blot, Over Expression, Inhibition, Immunoprecipitation, Positive Control, Chromatin Immunoprecipitation, Negative Control, shRNA, Knockdown, Standard Deviation, Two Tailed Test