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Cell Signaling Technology Inc rabbit anti ezh2
Rabbit Anti Ezh2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+ezh2+antibody/Ezh2+XP+Rabbit+mAb/pm41888115-297-35-41
Average 96 stars, based on 1128 article reviews

rabbit anti ezh2 - by Bioz Stars, 2026-10

96/100 stars

Images

Staining:

Article Title: EZH2 inhibition or genetic ablation suppresses cyst growth in autosomal dominant polycystic kidney disease.
Article Snippet: .. For EZH2 staining, a rabbit anti-EZH2 antibody (#5246S, 1:50, CST) was used. .. Ki-67 was stained with anti-Ki-67 (#ab15580, 1:100; Abcam).

Article Title: EZH2 inhibition or genetic ablation suppresses cyst growth in autosomal dominant polycystic kidney disease
Article Snippet: .. For EZH2 staining, a rabbit anti-EZH2 antibody (#5246S, 1:50, CST) was used. .. Ki-67 was stained with anti-Ki-67 (#ab15580, 1:100; Abcam).

Incubation:

Article Title: PHF19 drives PRC2 sub-nuclear compartmentalization to promote motility in TNBC cells
Article Snippet: .. The cells were then incubated with the rabbit anti-EZH2 antibody (5246, Cell signaling, USA) for 4 hours at RT, washed 3 times with PBST for 5 min and then incubated with Alexa FluorTM 647 secondary antibody (A-21245, ThermoFisher, USA) for 2 hours. ..

Article Title: PHF19 drives the formation of PRC2 clusters to enhance motility in TNBC cells.
Article Snippet: .. The cells were then incubated with the rabbit anti-EZH2 antibody (5246, Cell signaling, USA) for 4 h at RT, washed 3 times with PBST for 5 min and then incubated with Alexa Fluor 647 secondary antibody (A-21245, ThermoFisher, USA) for 2 h. The image processing function in Microscoop was used to generate a mask for EZH2 clusters, which automatically guided the photolabeling process within the masked regions across the entire cell chamber slide. .. Upon completion of the photolabeling process, the cells were quenched with the quencher in Synlight-RichTM kit (SYN-RI0106, Syncell, Taiwan) for 3 times wash, each for 5 min.

Article Title: Targeting IL-11R/EZH2 signaling axis as a therapeutic strategy for osteosarcoma lung metastases
Article Snippet: Antigen retrieval via heating with EDTA (pH 8.0; Zymed Laboratories) was followed by biotin and protein blocking (Dako). .. Expression of EZH2 was evaluated using a rabbit anti-EZH2 antibody (clone AC22; Cell Signaling Technology) diluted at 1:15 (vol/vol) and incubated for 45 min, followed by development using an LSAB + Kit (Dako). ..

Article Title: PHF19 drives the formation of PRC2 clusters to enhance motility in TNBC cells.
Article Snippet: The immunoprecipitation was performed in IP buffer, which was also used as wash buffer and consisted of 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM MgCl2, 0.5% NP-40, 10% glycerol, protease inhibitors (Roche) and phosphatase inhibitors. .. Equal amounts of nuclear lysates (0.4–0.8 mg per IP reaction as quantified by a Bradford assay), were mixed with 1 μg of rabbit anti-EZH2 antibody (5246, Cell signaling, USA) or 1 μg of rabbit (DA1E) mAb IgG XP Isotype Control (3900S, Cell Signaling USA) and incubated end-over-end for 16 h at 4 ◦ C. The immunocomplexes were retrieved by incubation with 30 μL protein Protein G Agarose beads (LGC SeraCare – KPL, 5720-0001) for 2 h at 4 ◦ C. The beads were subsequently washed five times with IP buffer before elution in 4× Bolt LDS Sample buffer (ThermoFischer Scientific, B0008) with 50 nM DTT, at 70 ◦ C for 10 min. .. For transient knockdowns, cells were reverse transfected using Lipofectamine RNAiMAX (Invitrogen) at a final concentration of 5nM total siRNA, according to manufacturer’s instructions.

Negative Control:

Article Title: Epigenetically silencing gluconeogenic enzyme PCK1 by EZH2 promotes renal tubulointerstitial fibrosis
Article Snippet: CUT&Tag experiments were performed following the procedures described in the CUT&Tag-seq section by using Hyperactive In-Situ ChIP Library Prep Kit for Illumina kit (Vazyme Biotech, TD901). .. Rabbit anti-EZH2 antibody (CST, 5246), the negative control rabbit IgG (CST, 3900) and the positive control Pol II antibody (CST, 2629) were used. ..

Positive Control:

Expressing:

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Control:

Image Search Results

A Changes in five types of alternative splicing events upon hnRNP A1/A2B1 knockout. Scatter plots show exon inclusion level differences between Hnrnpa1 f/f Hnrnpa2b1 f/f (WT) and Hnrnpa1 f/f Hnrnpa2b1 f/f Cd19 Cre/+ (double knockout, DKO) naïve B cells. Each dot represents a significantly altered splicing event (|inclusion level difference| > 20%, P < 0.05). B Lollipop plot showing the top 10 most significant exon-skipping events (ranked by P -value) in naïve B cells from DKO mice. The height of each lollipop indicates the inclusion level difference, and the circle size reflects statistical significance. C RNA expression changes of the top 10 most significant exon-skipping target genes (ranked by P -value) in follicular and Germinal center (GC) B cells from WT mice. Circle size and color intensity represent changes in FPKM values. Data from GEO: GSE15907 . D–H Alternative splicing of Ezh2 following hnRNP A1/A2B1 deletion. D Sashimi plot illustrating exon 14 splicing changes in Ezh2 in WT and DKO naïve B cells, showing both the full-length isoform and the exon 14-skipped isoform ( Ezh2Δ14 ). E Quantification of splice junction reads spanning exons 13–14, 14–15, and 13–15 in WT and DKO naïve B cells ( n = 3), data in ( E ) are from a single experiment (RNA-seq). F Schematic and primer design for detecting full-length ( Ezh2-FL ) and exon 14-skipped ( Ezh2Δ14 ) isoforms. G Semi-quantitative PCR showing the effect of single and double hnRNP knockouts on Ezh2 exon 14 skipping in WT and DKO naïve B cells, with accompanying gel image and the ratio of Ezh2Δ14 to Ezh2-FL . The data shown are representative images from two independent experiments. H Quantification of Ezh2-FL and Ezh2Δ14 expression normalized to β-actin in WT and DKO naïve B cells ( n = 2), the data shown here represent one representative set of statistical results from two independent experiments. I , J Western blot analysis detecting the abundance of H3K27me3 in B cells from WT, A1-SKO, A2B1-SKO, and DKO mice after 48 h of stimulation with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL). The data shown are representative images from two independent experiments. K Immunoblot analysis of H3K27me3 levels in WT and DKO B cells. Cells were pre-stimulated with anti-CD40 and anti-IgM and subsequently reconstituted with an empty vector (Vector), full-length EZH2 ( Ezh2 -FL), or the exon 14–skipped isoform ( Ezh2 Δ14). The data shown are representative images from two independent experiments. Each symbol represents an individual mouse ( E , H ). All data are shown as mean ± SEM. Results are representative of at least two independent experiments ( H ). Statistical significance was assessed using an unpaired two-tailed Student’s t -test ( E ).

Journal: Nature Communications

Article Title: HnRNP A1 and A2B1 enforce Ezh2 mRNA splicing to promote germinal center B cell responses

doi: 10.1038/s41467-026-74159-w

Figure Lengend Snippet: A Changes in five types of alternative splicing events upon hnRNP A1/A2B1 knockout. Scatter plots show exon inclusion level differences between Hnrnpa1 f/f Hnrnpa2b1 f/f (WT) and Hnrnpa1 f/f Hnrnpa2b1 f/f Cd19 Cre/+ (double knockout, DKO) naïve B cells. Each dot represents a significantly altered splicing event (|inclusion level difference| > 20%, P < 0.05). B Lollipop plot showing the top 10 most significant exon-skipping events (ranked by P -value) in naïve B cells from DKO mice. The height of each lollipop indicates the inclusion level difference, and the circle size reflects statistical significance. C RNA expression changes of the top 10 most significant exon-skipping target genes (ranked by P -value) in follicular and Germinal center (GC) B cells from WT mice. Circle size and color intensity represent changes in FPKM values. Data from GEO: GSE15907 . D–H Alternative splicing of Ezh2 following hnRNP A1/A2B1 deletion. D Sashimi plot illustrating exon 14 splicing changes in Ezh2 in WT and DKO naïve B cells, showing both the full-length isoform and the exon 14-skipped isoform ( Ezh2Δ14 ). E Quantification of splice junction reads spanning exons 13–14, 14–15, and 13–15 in WT and DKO naïve B cells ( n = 3), data in ( E ) are from a single experiment (RNA-seq). F Schematic and primer design for detecting full-length ( Ezh2-FL ) and exon 14-skipped ( Ezh2Δ14 ) isoforms. G Semi-quantitative PCR showing the effect of single and double hnRNP knockouts on Ezh2 exon 14 skipping in WT and DKO naïve B cells, with accompanying gel image and the ratio of Ezh2Δ14 to Ezh2-FL . The data shown are representative images from two independent experiments. H Quantification of Ezh2-FL and Ezh2Δ14 expression normalized to β-actin in WT and DKO naïve B cells ( n = 2), the data shown here represent one representative set of statistical results from two independent experiments. I , J Western blot analysis detecting the abundance of H3K27me3 in B cells from WT, A1-SKO, A2B1-SKO, and DKO mice after 48 h of stimulation with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL). The data shown are representative images from two independent experiments. K Immunoblot analysis of H3K27me3 levels in WT and DKO B cells. Cells were pre-stimulated with anti-CD40 and anti-IgM and subsequently reconstituted with an empty vector (Vector), full-length EZH2 ( Ezh2 -FL), or the exon 14–skipped isoform ( Ezh2 Δ14). The data shown are representative images from two independent experiments. Each symbol represents an individual mouse ( E , H ). All data are shown as mean ± SEM. Results are representative of at least two independent experiments ( H ). Statistical significance was assessed using an unpaired two-tailed Student’s t -test ( E ).

Article Snippet: Primary antibodies used were: β-actin (1:5000, Proteintech, 20536-1-AP), hnRNP A1 (1:1000, Santa Cruz Biotechnology, sc-32301), hnRNP A2B1 (1:1000, Santa Cruz Biotechnology, sc-53531), EZH2 (1:1000, ABclonal, A5743; A19577), H3K27me3 (1:1000, ABclonal, A22396), CDKN1A (1:1000, Cell Signaling Technology, 2947).

Techniques: Alternative Splicing, Knock-Out, Double Knockout, RNA Expression, RNA Sequencing, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Plasmid Preparation, Two Tailed Test

A Volcano plot showing differentially expressed genes identified by RNA-seq in Hnrnpa1 f/f Hnrnpa2b1 f/f (WT) and Hnrnpa1 f/f Hnrnpa2b1 f/f Cd19 Cre/+ (double knockout, DKO) B cells stimulated with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL) for 48 h. Differentially expressed genes are defined as those with |log 2 FC| > 1 and p < 0.05. CDKN1A is significantly upregulated in DKO B cells. Differential gene expression analysis for RNA-seq data was performed using DESeq2, which models count data based on the negative binomial distribution. Statistical significance was assessed using two-sided tests. P -values were adjusted for multiple comparisons using the Benjamini–Hochberg method to control the false discovery rate (FDR). Genes with an adjusted P value (FDR) < 0.05 were considered significantly differentially expressed. B qRT-PCR analysis of CDKN1A expression in naïve B cells, B cells stimulated with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL) for 48 h, and early Germinal center (GC) B cells isolated 5 days after NP-KLH/Alum immunization (naïve B : n = 6; anti-CD40 and anti-IgM: n = 6; early-GC: n = 5). C , D Western blot analysis of CDKN1A protein expression in unstimulated and 48-h-stimulated B cells ( n = 3). The data shown are represe n tative images from three independent experiments. E , F ChIP-qPCR analysis of Cdkn1a locus enriched by anti-H3K27me3 antibody in B cells from WT and DKO mice after 48 h of stimulation with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL). E A schematic representation of the Cdkn1a gene showing exons and the putative H3K27me3-enriched regions, P1 and P2. F ChIP-qPCR analysis validated the enrichment of H3K27me3 at the Cdkn1a genomic loci in WT and DKO B cells. Data are presented as fold enrichment relative to the WT IgG control. p < 0.0001( p = 2.06e-6). G , H CFSE dilution assay assessing proliferation of WT and DKO B cells following 72 h of anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL) stimulation ( n = 4). G Representative flow cytometry histograms showing CFSE dilution. H Quantitative analysis of CFSE dilution reflecting proliferation capacity ( n = 4; two independent experiments). Each symbol represents an individual mouse ( B , D , F , H ). Data are shown as mean ± SEM. Results shown are representative of at least three independent experiments ( B , D , F , H ). Statistical significance was determined using an unpaired two-tailed Student’s t -test ( B , D , H ) or one-way ANOVA followed by Tukey’s multiple comparisons test ( F ).

Journal: Nature Communications

Article Title: HnRNP A1 and A2B1 enforce Ezh2 mRNA splicing to promote germinal center B cell responses

doi: 10.1038/s41467-026-74159-w

Figure Lengend Snippet: A Volcano plot showing differentially expressed genes identified by RNA-seq in Hnrnpa1 f/f Hnrnpa2b1 f/f (WT) and Hnrnpa1 f/f Hnrnpa2b1 f/f Cd19 Cre/+ (double knockout, DKO) B cells stimulated with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL) for 48 h. Differentially expressed genes are defined as those with |log 2 FC| > 1 and p < 0.05. CDKN1A is significantly upregulated in DKO B cells. Differential gene expression analysis for RNA-seq data was performed using DESeq2, which models count data based on the negative binomial distribution. Statistical significance was assessed using two-sided tests. P -values were adjusted for multiple comparisons using the Benjamini–Hochberg method to control the false discovery rate (FDR). Genes with an adjusted P value (FDR) < 0.05 were considered significantly differentially expressed. B qRT-PCR analysis of CDKN1A expression in naïve B cells, B cells stimulated with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL) for 48 h, and early Germinal center (GC) B cells isolated 5 days after NP-KLH/Alum immunization (naïve B : n = 6; anti-CD40 and anti-IgM: n = 6; early-GC: n = 5). C , D Western blot analysis of CDKN1A protein expression in unstimulated and 48-h-stimulated B cells ( n = 3). The data shown are represe n tative images from three independent experiments. E , F ChIP-qPCR analysis of Cdkn1a locus enriched by anti-H3K27me3 antibody in B cells from WT and DKO mice after 48 h of stimulation with anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL). E A schematic representation of the Cdkn1a gene showing exons and the putative H3K27me3-enriched regions, P1 and P2. F ChIP-qPCR analysis validated the enrichment of H3K27me3 at the Cdkn1a genomic loci in WT and DKO B cells. Data are presented as fold enrichment relative to the WT IgG control. p < 0.0001( p = 2.06e-6). G , H CFSE dilution assay assessing proliferation of WT and DKO B cells following 72 h of anti-CD40 (1 μg/mL) and anti-IgM (2 μg/mL) stimulation ( n = 4). G Representative flow cytometry histograms showing CFSE dilution. H Quantitative analysis of CFSE dilution reflecting proliferation capacity ( n = 4; two independent experiments). Each symbol represents an individual mouse ( B , D , F , H ). Data are shown as mean ± SEM. Results shown are representative of at least three independent experiments ( B , D , F , H ). Statistical significance was determined using an unpaired two-tailed Student’s t -test ( B , D , H ) or one-way ANOVA followed by Tukey’s multiple comparisons test ( F ).

Techniques: RNA Sequencing, Double Knockout, Gene Expression, Control, Quantitative RT-PCR, Expressing, Isolation, Western Blot, ChIP-qPCR, Dilution Assay, Flow Cytometry, Two Tailed Test

Journal: Nature Communications

Article Title: HnRNP A1 and A2B1 enforce Ezh2 mRNA splicing to promote germinal center B cell responses

doi: 10.1038/s41467-026-74159-w

Techniques: Alternative Splicing, Knock-Out, Double Knockout, RNA Expression, RNA Sequencing, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Plasmid Preparation, Two Tailed Test

A RIP-qPCR analysis showing enrichment of Ezh2 transcripts associated with hnRNP A1 or hnRNP A2B1 in splenic B cells from WT mice, with B cells from Hnrnpa1 f/f Hnrnpa2b1 f/f Cd19 Cre/+ (double knockout, DKO) mice used as a control for RIP ( n = 2). Data are shown as mean ± SD from a single experiment. Statistical analysis was performed using an unpaired two-tailed Student’s t -test. B RBPmap prediction of hnRNP A1 and hnRNP A2B1 binding sites in Ezh2 . The analysis used exon 14 and part of intron 14 of Ezh2 as input. Underlined regions denote potential shared binding sites for hnRNP A1 and A2B1. C–E Construction and analysis of an Ezh2 minigene to assess exon 14 skipping upon site-directed mutation of predicted binding sites. C Schematic of the Ezh2 minigene and the design of mutations at predicted binding sites (M1, M2, and M3). Additional constructs include double (M1 + M3) and triple (M1 + M2 + M3) mutants. D , E WT and DKO B cells were infected with retroviruses carrying minigene constructs (WT, M1, M3, M1 + M3, and M1 + M2 + M3). 48 h after infection, GFP⁺ B cells were sorted by flow cytometry and subjected to RT-PCR analysis of Ezh2 splicing isoforms. The gel image shows the relative abundance of Ezh2Δ14 and Ezh2-FL isoforms. The data shown are representative images from two independent experiments. F–I RNA pull-down assay to evaluate binding of wild-type and mutant Ezh2 pre-RNAs to hnRNP A1 and A2B1. F Schematic of the RNA pull-down workflow. B cells were purified using CD19 magnetic beads, nuclear extracts were prepared, and biotin-labeled RNAs were pulled down using Streptavidin Magnetic Beads. G Biotin-labeled RNAs synthesized for pull-down: wild-type intron 14 RNA (I14–WT–Biotin), reverse complementary RNA (I14–Antisense–Biotin), triple mutant (I14–M1 + M2 + M3–Biotin), and M1-only mutant (I14–M1–Biotin). H Immunoblot analysis of proteins pulled down with biotin-labeled RNAs (I14–M1 + M2 + M3–Biotin), detecting hnRNP A1 and A2B1. I RNA pull-down assay was performed using the biotin-labeled RNA (I14–M1–Biotin), followed by immunoblotting to detect the precipitated hnRNP A1 and hnRNP A2B1 proteins. The data shown are representative images from two independent experiments. J–M RNA EMSA to determine direct binding of hnRNP A1 and A2B1 to wild-type or mutant Ezh2 pre-mRNA. J EMSA with hnRNP A1 and wild-type vs. M1 + M2 + M3 mutant Ezh2 pre-RNA. K EMSA with hnRNP A2B1 and wild-type vs. M1 + M2 + M3 mutant Ezh2 pre-RNA. L EMSA with hnRNP A1 and wild-type vs. M1 mutant Ezh2 pre-RNA. M EMSA with hnRNP A2B1 and wild-type vs. M1 mutant Ezh2 pre-RNA. The data shown are representative images from two independent experiments. All data are shown as mean ± SEM. Results shown are representative of three independent experiments ( A ). Statistical significance was assessed using an unpaired two-tailed Student’s t -test ( A ).

Journal: Nature Communications

Article Title: HnRNP A1 and A2B1 enforce Ezh2 mRNA splicing to promote germinal center B cell responses

doi: 10.1038/s41467-026-74159-w

Figure Lengend Snippet: A RIP-qPCR analysis showing enrichment of Ezh2 transcripts associated with hnRNP A1 or hnRNP A2B1 in splenic B cells from WT mice, with B cells from Hnrnpa1 f/f Hnrnpa2b1 f/f Cd19 Cre/+ (double knockout, DKO) mice used as a control for RIP ( n = 2). Data are shown as mean ± SD from a single experiment. Statistical analysis was performed using an unpaired two-tailed Student’s t -test. B RBPmap prediction of hnRNP A1 and hnRNP A2B1 binding sites in Ezh2 . The analysis used exon 14 and part of intron 14 of Ezh2 as input. Underlined regions denote potential shared binding sites for hnRNP A1 and A2B1. C–E Construction and analysis of an Ezh2 minigene to assess exon 14 skipping upon site-directed mutation of predicted binding sites. C Schematic of the Ezh2 minigene and the design of mutations at predicted binding sites (M1, M2, and M3). Additional constructs include double (M1 + M3) and triple (M1 + M2 + M3) mutants. D , E WT and DKO B cells were infected with retroviruses carrying minigene constructs (WT, M1, M3, M1 + M3, and M1 + M2 + M3). 48 h after infection, GFP⁺ B cells were sorted by flow cytometry and subjected to RT-PCR analysis of Ezh2 splicing isoforms. The gel image shows the relative abundance of Ezh2Δ14 and Ezh2-FL isoforms. The data shown are representative images from two independent experiments. F–I RNA pull-down assay to evaluate binding of wild-type and mutant Ezh2 pre-RNAs to hnRNP A1 and A2B1. F Schematic of the RNA pull-down workflow. B cells were purified using CD19 magnetic beads, nuclear extracts were prepared, and biotin-labeled RNAs were pulled down using Streptavidin Magnetic Beads. G Biotin-labeled RNAs synthesized for pull-down: wild-type intron 14 RNA (I14–WT–Biotin), reverse complementary RNA (I14–Antisense–Biotin), triple mutant (I14–M1 + M2 + M3–Biotin), and M1-only mutant (I14–M1–Biotin). H Immunoblot analysis of proteins pulled down with biotin-labeled RNAs (I14–M1 + M2 + M3–Biotin), detecting hnRNP A1 and A2B1. I RNA pull-down assay was performed using the biotin-labeled RNA (I14–M1–Biotin), followed by immunoblotting to detect the precipitated hnRNP A1 and hnRNP A2B1 proteins. The data shown are representative images from two independent experiments. J–M RNA EMSA to determine direct binding of hnRNP A1 and A2B1 to wild-type or mutant Ezh2 pre-mRNA. J EMSA with hnRNP A1 and wild-type vs. M1 + M2 + M3 mutant Ezh2 pre-RNA. K EMSA with hnRNP A2B1 and wild-type vs. M1 + M2 + M3 mutant Ezh2 pre-RNA. L EMSA with hnRNP A1 and wild-type vs. M1 mutant Ezh2 pre-RNA. M EMSA with hnRNP A2B1 and wild-type vs. M1 mutant Ezh2 pre-RNA. The data shown are representative images from two independent experiments. All data are shown as mean ± SEM. Results shown are representative of three independent experiments ( A ). Statistical significance was assessed using an unpaired two-tailed Student’s t -test ( A ).

Techniques: Double Knockout, Control, Two Tailed Test, Binding Assay, Mutagenesis, Construct, Infection, Flow Cytometry, Reverse Transcription Polymerase Chain Reaction, Pull Down Assay, Purification, Magnetic Beads, Labeling, Synthesized, Western Blot

Anti-transcription activity of γPNA1 with HDACi in lymphoma cells Relative fold change of c-Myc levels in U2932 cells measured by real-time PCR on day 2 after treatment with (A) γPNA1 and (B) ScR-γPNA2 in combination with romidepsin, entinostat, vorinostat, panobinostat, and belinostat. Results are presented as mean ± SEM and two-way ANOVA was used to determine the statistically significant difference between groups. Western blot analysis representing the change in c-MYC protein on day 2 after treatment with γPNA1 and ScR-γPNA2 in combination with (C) romidepsin, (D) entinostat, (E) vorinostat, (F) panobinostat, and (G) belinostat. ∗∗(C–F) Cyclophilin B was used as an endogenous control, and the same blots are presented in C–S3G. c-MYC, EZH2, and cyclophilin B were probed from the same blot. Results are presented as mean ± SEM, and the p value between groups was determined using one-way ANOVA.

Journal: Molecular Therapy. Nucleic Acids

Article Title: Combining anti-gene γPNA with small molecules and RNA inhibitors: A strategy to enhance anti-tumor efficacy

doi: 10.1016/j.omtn.2025.102804

Figure Lengend Snippet: Anti-transcription activity of γPNA1 with HDACi in lymphoma cells Relative fold change of c-Myc levels in U2932 cells measured by real-time PCR on day 2 after treatment with (A) γPNA1 and (B) ScR-γPNA2 in combination with romidepsin, entinostat, vorinostat, panobinostat, and belinostat. Results are presented as mean ± SEM and two-way ANOVA was used to determine the statistically significant difference between groups. Western blot analysis representing the change in c-MYC protein on day 2 after treatment with γPNA1 and ScR-γPNA2 in combination with (C) romidepsin, (D) entinostat, (E) vorinostat, (F) panobinostat, and (G) belinostat. ∗∗(C–F) Cyclophilin B was used as an endogenous control, and the same blots are presented in C–S3G. c-MYC, EZH2, and cyclophilin B were probed from the same blot. Results are presented as mean ± SEM, and the p value between groups was determined using one-way ANOVA.

Article Snippet: Primary antibodies for c-MYC (Cell Signaling Technology, #5605) and EZH2 (Cell Signaling Technology, #5246) were applied using a rabbit monoclonal antibody diluted in 3% BSA at 4°C overnight.

Techniques: Activity Assay, Real-time Polymerase Chain Reaction, Western Blot, Control

MYC/MAX inhibitors in combination with anti-transcription γPNA1 Cell viability of (A) U2932 and (B) Raji cells treated with increasing doses of MYC/MAX inhibitors (Myci975, EN4, 10058-F4, and sAJM589) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 72 h. Results are presented as mean ± SEM. The IC 50 (95% CI) values of MYC/MAX inhibitors alone and combination treatment of MYC/MAX with γPNA1 in (C) U2932 and (D) Raji cells. (E) Cell viability of γPNA1-treated U2932 and Raji cells at 8 μM concentration. Western blot analysis representing the change in c-MYC protein 72 h after treatment with γPNA1 and ScR-γPNA2 in combination with (F) Myci975, (G) EN4, (H) 10058-F4, and (I) sAJM589. ∗∗(F–I) Cyclophilin B was used as an endogenous control, and the same blots are presented in A–S7D. c-MYC, EZH2, and cyclophilin B were probed from the same blot. Results are presented as mean ± SEM, p value for one-way ANOVA.

Journal: Molecular Therapy. Nucleic Acids

Article Title: Combining anti-gene γPNA with small molecules and RNA inhibitors: A strategy to enhance anti-tumor efficacy

doi: 10.1016/j.omtn.2025.102804

Figure Lengend Snippet: MYC/MAX inhibitors in combination with anti-transcription γPNA1 Cell viability of (A) U2932 and (B) Raji cells treated with increasing doses of MYC/MAX inhibitors (Myci975, EN4, 10058-F4, and sAJM589) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 72 h. Results are presented as mean ± SEM. The IC 50 (95% CI) values of MYC/MAX inhibitors alone and combination treatment of MYC/MAX with γPNA1 in (C) U2932 and (D) Raji cells. (E) Cell viability of γPNA1-treated U2932 and Raji cells at 8 μM concentration. Western blot analysis representing the change in c-MYC protein 72 h after treatment with γPNA1 and ScR-γPNA2 in combination with (F) Myci975, (G) EN4, (H) 10058-F4, and (I) sAJM589. ∗∗(F–I) Cyclophilin B was used as an endogenous control, and the same blots are presented in A–S7D. c-MYC, EZH2, and cyclophilin B were probed from the same blot. Results are presented as mean ± SEM, p value for one-way ANOVA.

Techniques: Concentration Assay, Western Blot, Control

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