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ezh2 antibody  (NSJ Bioreagents)


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    Structured Review

    NSJ Bioreagents ezh2 antibody
    Ezh2 Antibody, supplied by NSJ Bioreagents, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ezh2+antibody/EZH2+Antibody/custom%40f40221%4042711427
    Average 91 stars, based on 8 article reviews
    ezh2 antibody - by Bioz Stars, 2026-11
    91/100 stars

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    Related Articles

    Binding Assay:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    Staining:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    Blocking Assay:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    Proximity Ligation Assay:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    In Situ:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    Amplification:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    Ligation:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an

    Incubation:

    Article Title: Tumor-associated antigen PRAME exhibits dualistic functions that are targetable in diffuse large B cell lymphoma
    Article Snippet: formaldehyde and embedded into paraffin tissue blocks. Samples were incubated with primary antibodies (rabbit anti-PRAME antibody: Abcam EPR20330 and mouse anti-EZH2 antibody: Thermo Fisher Scientific 144CT2.1.1.5) for 1 hour at 37°C. PLA probes (Duolink In Situ PLA Probe Anti-Mouse MINUS and Anti-Rabbit PLUS, MilliporeSigma) were incubated for 1 hour at 37°C. Then, ligation (30 minutes at 37°C) an



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    Hypoxia increases expression of <t>EZH2,</t> H3K27me3 and survivin. (A) Immunoblots of WCEs from U2OS, HeLa and MRC5 lines cultured under normoxic or hypoxic environments (24 h). Blots were immunoprobed with <t>anti-EZH2,</t> anti-H3K27me3 and anti-survivin antibodies. Anti-Hif1a used to prove the hypoxic state had been induced, and anti-tubulin was used as a loading control. (B–D) Quantification of immunoblots represented in A from three independent experiments demonstrating that EZH2, H3K27me3 and survivin are all more abundant under hypoxia. Data presented are means±s.d. * P <0.05, ** P <0.01, *** P <0.001 (two-way ANOVA with Tukey's multiple comparisons post test).
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    Hypoxia increases expression of <t>EZH2,</t> H3K27me3 and survivin. (A) Immunoblots of WCEs from U2OS, HeLa and MRC5 lines cultured under normoxic or hypoxic environments (24 h). Blots were immunoprobed with <t>anti-EZH2,</t> anti-H3K27me3 and anti-survivin antibodies. Anti-Hif1a used to prove the hypoxic state had been induced, and anti-tubulin was used as a loading control. (B–D) Quantification of immunoblots represented in A from three independent experiments demonstrating that EZH2, H3K27me3 and survivin are all more abundant under hypoxia. Data presented are means±s.d. * P <0.05, ** P <0.01, *** P <0.001 (two-way ANOVA with Tukey's multiple comparisons post test).
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    (A-C) Images and quantification of <t>Ezh2</t> immunofluorescence in WT and Sun2 KO dermal fibroblasts cultured on soft or stiff substrates. (A) Scale bar = 10 μ m. (B) Quantification of nuclear Ezh2 intensity. N = 2, n soft = 21–37, n stiff = 20–24. Significance was assessed using a two-tailed Mann–Whitney U test. (C) qPCR analysis of Ezh2 mRNA expression in WT or Sun2 KO fibroblasts on soft or stiff substrates. N = 3. Significance was assessed using a two-tailed Mann–Whitney U test. (D-E) Schematic and analysis of WT and Sun2 KO dermal fibroblasts plated on soft or stiff substrates for 24 h, followed by 24 h treatment with the Ezh2 inhibitor GSK343 or DMSO (Day 1), and collection for qPCR (Day 2). N = 3 independent experiments. Statistical significance was assessed using one-way ANOVA. ns, not significant; p < 0.05, * p < 0.01, ** p < 0.001, *** p < 0.0001. (F) Proposed model for SUN2–LINC–PRC2–dependent control of profibrotic gene expression in dermal fibroblasts. In quiescent WT fibroblasts, fibrotic genes are repressed. Upon mechanical stimulation of WT cells, cytoskeletal tension transmitted through LINC complexes promotes lamin stretching and altered Ezh2-driven epigenetic remodeling to activate transcription, repress transcriptional activators, and promote enhancer-licensing. In Sun2 KO dermal fibroblasts,loss of LINC complexes blunts this mechanotransduction despite cytoskeletal activation.
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    Image Search Results


    Detection of protein-protein interaction between AR and EZH2 by co-IP-western blotting

    Journal: BMC Cancer

    Article Title: Investigation of the significance and role of androgen receptor expression in basal/squamous type urothelial carcinoma cell line J82 cells

    doi: 10.1186/s12885-026-16533-x

    Figure Lengend Snippet: Detection of protein-protein interaction between AR and EZH2 by co-IP-western blotting

    Article Snippet: The dilutions of primary antibodies used in this study were as follows: FLAG (FUJIFILM Wako Pure Chemical Corporation, Osaka, Japan), 1:10000; GAPDH (Proteintech, Tokyo, Japan), 1:20000; p21 (Proteintech, Tokyo, Japan), 1:10000; EZH2 (Proteintech, Tokyo, Japan), 1:10000.

    Techniques: Co-Immunoprecipitation Assay, Western Blot

    Hypoxia increases expression of EZH2, H3K27me3 and survivin. (A) Immunoblots of WCEs from U2OS, HeLa and MRC5 lines cultured under normoxic or hypoxic environments (24 h). Blots were immunoprobed with anti-EZH2, anti-H3K27me3 and anti-survivin antibodies. Anti-Hif1a used to prove the hypoxic state had been induced, and anti-tubulin was used as a loading control. (B–D) Quantification of immunoblots represented in A from three independent experiments demonstrating that EZH2, H3K27me3 and survivin are all more abundant under hypoxia. Data presented are means±s.d. * P <0.05, ** P <0.01, *** P <0.001 (two-way ANOVA with Tukey's multiple comparisons post test).

    Journal: Journal of Cell Science

    Article Title: Interplay between nuclear survivin and the PRC2 complex and its impact on H3K27me3-directed transcriptional repression

    doi: 10.1242/jcs.264572

    Figure Lengend Snippet: Hypoxia increases expression of EZH2, H3K27me3 and survivin. (A) Immunoblots of WCEs from U2OS, HeLa and MRC5 lines cultured under normoxic or hypoxic environments (24 h). Blots were immunoprobed with anti-EZH2, anti-H3K27me3 and anti-survivin antibodies. Anti-Hif1a used to prove the hypoxic state had been induced, and anti-tubulin was used as a loading control. (B–D) Quantification of immunoblots represented in A from three independent experiments demonstrating that EZH2, H3K27me3 and survivin are all more abundant under hypoxia. Data presented are means±s.d. * P <0.05, ** P <0.01, *** P <0.001 (two-way ANOVA with Tukey's multiple comparisons post test).

    Article Snippet: The following primary antibodies were used at 1:200: anti-survivin (Cell Signaling Technologies 71G4B7 or 6E4), anti-H3K27Me3 (Abcam, Ab192985 ), anti-EZH2 [Cell Signalling Technologies (CST), D269].

    Techniques: Expressing, Western Blot, Cell Culture, Control

    Survivin and EZH2 interact. (A) Immunoprecipitation was carried out using whole MRC5 extracts using anti-survivin (C60), anti-EZH2, mouse IgG antibodies (negative control). Co-immunoprecipitation was assessed with the alternative antibodies. Co-immunoprecipitation of EZH2 with survivin was evident when anti-EZH2 was used to immunoprecipitate but not when the anti-survivin (C60) antibody was used. (B) GST pulldown assay was carried out with WCEs prepared from RPE cells expressing GST (negative control), GST–survivin and various GST-tagged survivin truncations, (numbering indicating amino acids), used as bait. (C) Quantification of interactions represented in B. EZH2 binds mainly to the first 90 amino acids of survivin. Data are mean±s.d. from three independent experiments. *** P <0.001; **** P <0.0001; ns, not significant (one-way ANOVA with Dunnett's post hoc test). (D) Immunoprecipitation was carried out as in A but using anti-H3K27me3 specific antibodies, rather than anti-EZH2. Co-immunoprecipitation of survivin and H3K27me3 was evident in reciprocal samples. (E) The GST pulldown experiment as in B was repeated using RPE cell lysates with GST or GST–survivin, and interaction with H3K27me3 determined by immunoblotting. (F) Quantification of data represented in E, normalised to the GST or GST–survivin. Data are mean±s.d., n =3. *** P <0.001 (unpaired two-tailed Student's t -test). Blots in A and D are representative of three repeats. Inputs are 7.5%.

    Journal: Journal of Cell Science

    Article Title: Interplay between nuclear survivin and the PRC2 complex and its impact on H3K27me3-directed transcriptional repression

    doi: 10.1242/jcs.264572

    Figure Lengend Snippet: Survivin and EZH2 interact. (A) Immunoprecipitation was carried out using whole MRC5 extracts using anti-survivin (C60), anti-EZH2, mouse IgG antibodies (negative control). Co-immunoprecipitation was assessed with the alternative antibodies. Co-immunoprecipitation of EZH2 with survivin was evident when anti-EZH2 was used to immunoprecipitate but not when the anti-survivin (C60) antibody was used. (B) GST pulldown assay was carried out with WCEs prepared from RPE cells expressing GST (negative control), GST–survivin and various GST-tagged survivin truncations, (numbering indicating amino acids), used as bait. (C) Quantification of interactions represented in B. EZH2 binds mainly to the first 90 amino acids of survivin. Data are mean±s.d. from three independent experiments. *** P <0.001; **** P <0.0001; ns, not significant (one-way ANOVA with Dunnett's post hoc test). (D) Immunoprecipitation was carried out as in A but using anti-H3K27me3 specific antibodies, rather than anti-EZH2. Co-immunoprecipitation of survivin and H3K27me3 was evident in reciprocal samples. (E) The GST pulldown experiment as in B was repeated using RPE cell lysates with GST or GST–survivin, and interaction with H3K27me3 determined by immunoblotting. (F) Quantification of data represented in E, normalised to the GST or GST–survivin. Data are mean±s.d., n =3. *** P <0.001 (unpaired two-tailed Student's t -test). Blots in A and D are representative of three repeats. Inputs are 7.5%.

    Article Snippet: The following primary antibodies were used at 1:200: anti-survivin (Cell Signaling Technologies 71G4B7 or 6E4), anti-H3K27Me3 (Abcam, Ab192985 ), anti-EZH2 [Cell Signalling Technologies (CST), D269].

    Techniques: Immunoprecipitation, Negative Control, GST Pulldown Assay, Expressing, Western Blot, Two Tailed Test

    (A-C) Images and quantification of Ezh2 immunofluorescence in WT and Sun2 KO dermal fibroblasts cultured on soft or stiff substrates. (A) Scale bar = 10 μ m. (B) Quantification of nuclear Ezh2 intensity. N = 2, n soft = 21–37, n stiff = 20–24. Significance was assessed using a two-tailed Mann–Whitney U test. (C) qPCR analysis of Ezh2 mRNA expression in WT or Sun2 KO fibroblasts on soft or stiff substrates. N = 3. Significance was assessed using a two-tailed Mann–Whitney U test. (D-E) Schematic and analysis of WT and Sun2 KO dermal fibroblasts plated on soft or stiff substrates for 24 h, followed by 24 h treatment with the Ezh2 inhibitor GSK343 or DMSO (Day 1), and collection for qPCR (Day 2). N = 3 independent experiments. Statistical significance was assessed using one-way ANOVA. ns, not significant; p < 0.05, * p < 0.01, ** p < 0.001, *** p < 0.0001. (F) Proposed model for SUN2–LINC–PRC2–dependent control of profibrotic gene expression in dermal fibroblasts. In quiescent WT fibroblasts, fibrotic genes are repressed. Upon mechanical stimulation of WT cells, cytoskeletal tension transmitted through LINC complexes promotes lamin stretching and altered Ezh2-driven epigenetic remodeling to activate transcription, repress transcriptional activators, and promote enhancer-licensing. In Sun2 KO dermal fibroblasts,loss of LINC complexes blunts this mechanotransduction despite cytoskeletal activation.

    Journal: bioRxiv

    Article Title: SUN2 mediates epigenetic remodeling to drive mechanotransduction during skin fibrosis

    doi: 10.64898/2026.03.19.712957

    Figure Lengend Snippet: (A-C) Images and quantification of Ezh2 immunofluorescence in WT and Sun2 KO dermal fibroblasts cultured on soft or stiff substrates. (A) Scale bar = 10 μ m. (B) Quantification of nuclear Ezh2 intensity. N = 2, n soft = 21–37, n stiff = 20–24. Significance was assessed using a two-tailed Mann–Whitney U test. (C) qPCR analysis of Ezh2 mRNA expression in WT or Sun2 KO fibroblasts on soft or stiff substrates. N = 3. Significance was assessed using a two-tailed Mann–Whitney U test. (D-E) Schematic and analysis of WT and Sun2 KO dermal fibroblasts plated on soft or stiff substrates for 24 h, followed by 24 h treatment with the Ezh2 inhibitor GSK343 or DMSO (Day 1), and collection for qPCR (Day 2). N = 3 independent experiments. Statistical significance was assessed using one-way ANOVA. ns, not significant; p < 0.05, * p < 0.01, ** p < 0.001, *** p < 0.0001. (F) Proposed model for SUN2–LINC–PRC2–dependent control of profibrotic gene expression in dermal fibroblasts. In quiescent WT fibroblasts, fibrotic genes are repressed. Upon mechanical stimulation of WT cells, cytoskeletal tension transmitted through LINC complexes promotes lamin stretching and altered Ezh2-driven epigenetic remodeling to activate transcription, repress transcriptional activators, and promote enhancer-licensing. In Sun2 KO dermal fibroblasts,loss of LINC complexes blunts this mechanotransduction despite cytoskeletal activation.

    Article Snippet: Primary antibody diluted in blocking solution – SUN2, 1:200 (Abcam, AB124916), YAP, 1:200 (CST, 4912S), LaminA/C (Abcam, AB133256), and/or Ezh2, 1:200 (CST, 5246T) was incubated overnight at 4°C.

    Techniques: Immunofluorescence, Cell Culture, Two Tailed Test, MANN-WHITNEY, Expressing, Control, Gene Expression, Activation Assay