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u2932 cells  (MedChemExpress)


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    MedChemExpress u2932 cells
    Design of anti-transcription γPNA and combination treatments to target the c-Myc oncogene (A) Schematic representation of gamma peptide nucleic (γPNA)-mediated inhibition of human c-Myc transcription and target site (NCBI database RefSeq: NG_007161.2 ). (B) Design of γPNA conjugated with nuclear localization signal (NLS) to target the indicated sites. ScR-γPNA2 is the scramble control. (C) Graphic representation of combination treatments with anti-transcription, γPNA1. The combination treatments include histone deacetylase inhibitors (HDACis), MYC/MAX inhibitors, small interfering RNA (siRNA), and small molecules targeting other pathways. (D) Polymerase chain reaction (PCR)-based amplicon assay to confirm binding of γPNA1 to the target site in <t>U2932</t> cells. Amplicon assay after treatment of γPNA1 and ScR-γPNA2 with HDACi. (E) The graph represents quantification of γPNA1 and ScR-γPNA2 amplicon in combination with HDACi. (F) The graph represents the quantification of amplicon assay from class I HDACi with γPNA1. Results are presented as mean ± SEM. One-way ANOVA was used to determine the statistically significant difference between groups.
    U2932 Cells, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/u2932+cells/pmc12796863-242-0-7?v=MedChemExpress
    Average 95 stars, based on 93 article reviews
    u2932 cells - by Bioz Stars, 2026-07
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    Images

    1) Product Images from "Combining anti-gene γPNA with small molecules and RNA inhibitors: A strategy to enhance anti-tumor efficacy"

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

    Journal: Molecular Therapy. Nucleic Acids

    doi: 10.1016/j.omtn.2025.102804

    Design of anti-transcription γPNA and combination treatments to target the c-Myc oncogene (A) Schematic representation of gamma peptide nucleic (γPNA)-mediated inhibition of human c-Myc transcription and target site (NCBI database RefSeq: NG_007161.2 ). (B) Design of γPNA conjugated with nuclear localization signal (NLS) to target the indicated sites. ScR-γPNA2 is the scramble control. (C) Graphic representation of combination treatments with anti-transcription, γPNA1. The combination treatments include histone deacetylase inhibitors (HDACis), MYC/MAX inhibitors, small interfering RNA (siRNA), and small molecules targeting other pathways. (D) Polymerase chain reaction (PCR)-based amplicon assay to confirm binding of γPNA1 to the target site in U2932 cells. Amplicon assay after treatment of γPNA1 and ScR-γPNA2 with HDACi. (E) The graph represents quantification of γPNA1 and ScR-γPNA2 amplicon in combination with HDACi. (F) The graph represents the quantification of amplicon assay from class I HDACi with γPNA1. Results are presented as mean ± SEM. One-way ANOVA was used to determine the statistically significant difference between groups.
    Figure Legend Snippet: Design of anti-transcription γPNA and combination treatments to target the c-Myc oncogene (A) Schematic representation of gamma peptide nucleic (γPNA)-mediated inhibition of human c-Myc transcription and target site (NCBI database RefSeq: NG_007161.2 ). (B) Design of γPNA conjugated with nuclear localization signal (NLS) to target the indicated sites. ScR-γPNA2 is the scramble control. (C) Graphic representation of combination treatments with anti-transcription, γPNA1. The combination treatments include histone deacetylase inhibitors (HDACis), MYC/MAX inhibitors, small interfering RNA (siRNA), and small molecules targeting other pathways. (D) Polymerase chain reaction (PCR)-based amplicon assay to confirm binding of γPNA1 to the target site in U2932 cells. Amplicon assay after treatment of γPNA1 and ScR-γPNA2 with HDACi. (E) The graph represents quantification of γPNA1 and ScR-γPNA2 amplicon in combination with HDACi. (F) The graph represents the quantification of amplicon assay from class I HDACi with γPNA1. Results are presented as mean ± SEM. One-way ANOVA was used to determine the statistically significant difference between groups.

    Techniques Used: Inhibition, Control, Histone Deacetylase Assay, Small Interfering RNA, Polymerase Chain Reaction, Amplification, Binding Assay

    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.
    Figure Legend 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.

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

    Cell viability of Histone deacetylase inhibitors in combination with γPNA1 (A) Cell viability of U2932 cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (B) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in U2932 cells. (C) Cell viability of Raji cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (D) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in Raji cells.
    Figure Legend Snippet: Cell viability of Histone deacetylase inhibitors in combination with γPNA1 (A) Cell viability of U2932 cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (B) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in U2932 cells. (C) Cell viability of Raji cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (D) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in Raji cells.

    Techniques Used: Histone Deacetylase Assay

    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.
    Figure Legend 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 Used: Concentration Assay, Western Blot, Control

    Efficacy of small molecules targeting other pathways with anti-transcription γPNA1 (A) Cell viability of U2932 and Raji cells treated with increasing doses JQ1 (BRD4 inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (B) Cell viability of U2932 and Raji cells treated with increasing doses of sapnisertid (mTOR inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (C) Cell viability of MDA-MB-231 cells treated with increasing doses of dinaciclib (CDK inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (D) The IC 50 (95% CI) values of small molecule inhibitors alone and in combination with γPNA1. (A–C) Results are presented as mean ± SEM.
    Figure Legend Snippet: Efficacy of small molecules targeting other pathways with anti-transcription γPNA1 (A) Cell viability of U2932 and Raji cells treated with increasing doses JQ1 (BRD4 inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (B) Cell viability of U2932 and Raji cells treated with increasing doses of sapnisertid (mTOR inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (C) Cell viability of MDA-MB-231 cells treated with increasing doses of dinaciclib (CDK inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (D) The IC 50 (95% CI) values of small molecule inhibitors alone and in combination with γPNA1. (A–C) Results are presented as mean ± SEM.

    Techniques Used:



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    Image Search Results


    Design of anti-transcription γPNA and combination treatments to target the c-Myc oncogene (A) Schematic representation of gamma peptide nucleic (γPNA)-mediated inhibition of human c-Myc transcription and target site (NCBI database RefSeq: NG_007161.2 ). (B) Design of γPNA conjugated with nuclear localization signal (NLS) to target the indicated sites. ScR-γPNA2 is the scramble control. (C) Graphic representation of combination treatments with anti-transcription, γPNA1. The combination treatments include histone deacetylase inhibitors (HDACis), MYC/MAX inhibitors, small interfering RNA (siRNA), and small molecules targeting other pathways. (D) Polymerase chain reaction (PCR)-based amplicon assay to confirm binding of γPNA1 to the target site in U2932 cells. Amplicon assay after treatment of γPNA1 and ScR-γPNA2 with HDACi. (E) The graph represents quantification of γPNA1 and ScR-γPNA2 amplicon in combination with HDACi. (F) The graph represents the quantification of amplicon assay from class I HDACi with γPNA1. Results are presented as mean ± SEM. One-way ANOVA was used to determine the statistically significant difference between groups.

    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: Design of anti-transcription γPNA and combination treatments to target the c-Myc oncogene (A) Schematic representation of gamma peptide nucleic (γPNA)-mediated inhibition of human c-Myc transcription and target site (NCBI database RefSeq: NG_007161.2 ). (B) Design of γPNA conjugated with nuclear localization signal (NLS) to target the indicated sites. ScR-γPNA2 is the scramble control. (C) Graphic representation of combination treatments with anti-transcription, γPNA1. The combination treatments include histone deacetylase inhibitors (HDACis), MYC/MAX inhibitors, small interfering RNA (siRNA), and small molecules targeting other pathways. (D) Polymerase chain reaction (PCR)-based amplicon assay to confirm binding of γPNA1 to the target site in U2932 cells. Amplicon assay after treatment of γPNA1 and ScR-γPNA2 with HDACi. (E) The graph represents quantification of γPNA1 and ScR-γPNA2 amplicon in combination with HDACi. (F) The graph represents the quantification of amplicon assay from class I HDACi with γPNA1. Results are presented as mean ± SEM. One-way ANOVA was used to determine the statistically significant difference between groups.

    Article Snippet: U2932 cells were treated with HDACi: panobinostat (MedchemExpress, #HY-10224; 30 nM), belinostat (MedchemExpress, #HY-10225; 2.5 μM), entinostat (MedchemExpress, #HY-12163; 10 μM, romidepsin (Sigma-Aldrich, #SML1175; 10 nM), and vorinostat (Selleckchem, #S1047; 2.5 μM) for 24 h followed by PBS, γPNA1, and ScR-γPNA2 at 3 μM for 48 h cotreatment.

    Techniques: Inhibition, Control, Histone Deacetylase Assay, Small Interfering RNA, Polymerase Chain Reaction, Amplification, Binding Assay

    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: U2932 cells were treated with HDACi: panobinostat (MedchemExpress, #HY-10224; 30 nM), belinostat (MedchemExpress, #HY-10225; 2.5 μM), entinostat (MedchemExpress, #HY-12163; 10 μM, romidepsin (Sigma-Aldrich, #SML1175; 10 nM), and vorinostat (Selleckchem, #S1047; 2.5 μM) for 24 h followed by PBS, γPNA1, and ScR-γPNA2 at 3 μM for 48 h cotreatment.

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

    Cell viability of Histone deacetylase inhibitors in combination with γPNA1 (A) Cell viability of U2932 cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (B) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in U2932 cells. (C) Cell viability of Raji cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (D) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in Raji cells.

    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: Cell viability of Histone deacetylase inhibitors in combination with γPNA1 (A) Cell viability of U2932 cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (B) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in U2932 cells. (C) Cell viability of Raji cells treated with increasing doses of HDACi (romidepsin, entinostat, vorinostat, panobinostat, and belinostat) alone and in combination with γPNA1 and ScR-γPNA2 (8 μM) for 48 h. Results are presented as mean ± SEM. (D) The IC 50 ± SEM values of HDACi and combination treatment of HDACi with γPNA1 in Raji cells.

    Article Snippet: U2932 cells were treated with HDACi: panobinostat (MedchemExpress, #HY-10224; 30 nM), belinostat (MedchemExpress, #HY-10225; 2.5 μM), entinostat (MedchemExpress, #HY-12163; 10 μM, romidepsin (Sigma-Aldrich, #SML1175; 10 nM), and vorinostat (Selleckchem, #S1047; 2.5 μM) for 24 h followed by PBS, γPNA1, and ScR-γPNA2 at 3 μM for 48 h cotreatment.

    Techniques: Histone Deacetylase Assay

    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.

    Article Snippet: U2932 cells were treated with HDACi: panobinostat (MedchemExpress, #HY-10224; 30 nM), belinostat (MedchemExpress, #HY-10225; 2.5 μM), entinostat (MedchemExpress, #HY-12163; 10 μM, romidepsin (Sigma-Aldrich, #SML1175; 10 nM), and vorinostat (Selleckchem, #S1047; 2.5 μM) for 24 h followed by PBS, γPNA1, and ScR-γPNA2 at 3 μM for 48 h cotreatment.

    Techniques: Concentration Assay, Western Blot, Control

    Efficacy of small molecules targeting other pathways with anti-transcription γPNA1 (A) Cell viability of U2932 and Raji cells treated with increasing doses JQ1 (BRD4 inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (B) Cell viability of U2932 and Raji cells treated with increasing doses of sapnisertid (mTOR inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (C) Cell viability of MDA-MB-231 cells treated with increasing doses of dinaciclib (CDK inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (D) The IC 50 (95% CI) values of small molecule inhibitors alone and in combination with γPNA1. (A–C) Results are presented as mean ± SEM.

    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: Efficacy of small molecules targeting other pathways with anti-transcription γPNA1 (A) Cell viability of U2932 and Raji cells treated with increasing doses JQ1 (BRD4 inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (B) Cell viability of U2932 and Raji cells treated with increasing doses of sapnisertid (mTOR inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (C) Cell viability of MDA-MB-231 cells treated with increasing doses of dinaciclib (CDK inhibitor) alone and with γPNA1 and ScR-γPNA2 for 48 h. (D) The IC 50 (95% CI) values of small molecule inhibitors alone and in combination with γPNA1. (A–C) Results are presented as mean ± SEM.

    Article Snippet: U2932 cells were treated with HDACi: panobinostat (MedchemExpress, #HY-10224; 30 nM), belinostat (MedchemExpress, #HY-10225; 2.5 μM), entinostat (MedchemExpress, #HY-12163; 10 μM, romidepsin (Sigma-Aldrich, #SML1175; 10 nM), and vorinostat (Selleckchem, #S1047; 2.5 μM) for 24 h followed by PBS, γPNA1, and ScR-γPNA2 at 3 μM for 48 h cotreatment.

    Techniques:

    LSD1 inhibition promotes M1-like polarization of monocyte-derived macrophages. A Riva cells expressing either control vector or LMP1 were treated with ORY1001 (10 µM) for 24 or 48 h, and the conditioned media were collected. The media were added to THP-1-derived monocytes and cultured for 72 h. The expression of M1 and M2 macrophage markers was assessed by qPCR. B Under the same conditions, the expression of M1 and M2 markers was validated by flow cytometry. C-D CD14+ monocytes were isolated from PBMCs and differentiated into M0 macrophages. These cells were then cultured with conditioned media from ORY1001-treated Riva cells, followed by analysis of M1/M2 marker expression using qPCR ( C ) and flow cytometry D . E–F To assess whether these effects were conserved in additional EBV-related models, LMP1-expressing U2932 cells and primary EBV+ DLBCL cells were treated with ORY1001 (10 µM), and conditioned media were collected and applied to THP-1-derived monocytes or primary CD14+ monocytes. After 72 h of culture, M1- and M2-associated markers were quantified by qPCR ( E ), and surface expression of CD80 and CD163 was analyzed by flow cytometry F . Significant differences between control and treated groups are indicated as * ( p < 0.05), ** ( p < 0.01) and *** ( p < 0.001). Statistical significance for 24-hour treatments was evaluated using unpaired two-tailed t-test

    Journal: Cell Communication and Signaling : CCS

    Article Title: ORY1001 enhances anti-tumor immunity via CXCL10-mediated macrophage modulation in EBV-positive DLBCL

    doi: 10.1186/s12964-025-02614-0

    Figure Lengend Snippet: LSD1 inhibition promotes M1-like polarization of monocyte-derived macrophages. A Riva cells expressing either control vector or LMP1 were treated with ORY1001 (10 µM) for 24 or 48 h, and the conditioned media were collected. The media were added to THP-1-derived monocytes and cultured for 72 h. The expression of M1 and M2 macrophage markers was assessed by qPCR. B Under the same conditions, the expression of M1 and M2 markers was validated by flow cytometry. C-D CD14+ monocytes were isolated from PBMCs and differentiated into M0 macrophages. These cells were then cultured with conditioned media from ORY1001-treated Riva cells, followed by analysis of M1/M2 marker expression using qPCR ( C ) and flow cytometry D . E–F To assess whether these effects were conserved in additional EBV-related models, LMP1-expressing U2932 cells and primary EBV+ DLBCL cells were treated with ORY1001 (10 µM), and conditioned media were collected and applied to THP-1-derived monocytes or primary CD14+ monocytes. After 72 h of culture, M1- and M2-associated markers were quantified by qPCR ( E ), and surface expression of CD80 and CD163 was analyzed by flow cytometry F . Significant differences between control and treated groups are indicated as * ( p < 0.05), ** ( p < 0.01) and *** ( p < 0.001). Statistical significance for 24-hour treatments was evaluated using unpaired two-tailed t-test

    Article Snippet: The Riva and U2932 cell lines were obtained from the Leibniz-Institut DSMZ-Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (Braunschweig, Germany).

    Techniques: Inhibition, Derivative Assay, Expressing, Control, Plasmid Preparation, Cell Culture, Flow Cytometry, Isolation, Marker, Two Tailed Test

    Preliminary single dose treatment (50 µg/mL) with stingless bee propolis extracts and its effect on cancer cell viability. ( A ) Comparison of the effects of ethanol and ethyl acetate extracts from five stingless bee species on the viability of three cancer cell lines (U2932, H1975, and EJ). Statistical significance is indicated. ***, p < 0.001; **, p < 0.01; *, p < 0.05; n.s., non-significant. ( B ) Comparison of the effects of ethanol propolis extracts (50 µg/mL) from five stingless bee species ( H. itama , T. melanoleuca , T. binghami , G. thoracica , and L. canifrons ) on the viability of five cancer cell lines (U2932, H1975, OCI-LY3, HT, and EJ). The heatmap represents post-treatment cell viability (%), where lower values (red) indicate stronger cytotoxic effects.

    Journal: Scientific Reports

    Article Title: Anti-cancer activity of propolis extracts from stingless bees of Brunei Darussalam

    doi: 10.1038/s41598-025-32628-0

    Figure Lengend Snippet: Preliminary single dose treatment (50 µg/mL) with stingless bee propolis extracts and its effect on cancer cell viability. ( A ) Comparison of the effects of ethanol and ethyl acetate extracts from five stingless bee species on the viability of three cancer cell lines (U2932, H1975, and EJ). Statistical significance is indicated. ***, p < 0.001; **, p < 0.01; *, p < 0.05; n.s., non-significant. ( B ) Comparison of the effects of ethanol propolis extracts (50 µg/mL) from five stingless bee species ( H. itama , T. melanoleuca , T. binghami , G. thoracica , and L. canifrons ) on the viability of five cancer cell lines (U2932, H1975, OCI-LY3, HT, and EJ). The heatmap represents post-treatment cell viability (%), where lower values (red) indicate stronger cytotoxic effects.

    Article Snippet: DLBCL U2932 cell line (Catalog no. ACC 633, DSMZ, Germany) were maintained in modified RPMI supplemented with 10% fetal bovine serum, 1% L-glutamine, and 1% penicillin-streptomycin.

    Techniques: Comparison

    Dose-dependent and time-dependent response of stingless bee ethanol extracts on cancer cell lines. ( A ) Heatmap of IC50 values across cell lines (EJ, H1975, U2932, HT, and OCI-LY3) and bee species ethanol extracts ( T. melanocephala , H. itama , L. canifrons , G. thoracica , and T. binghami ). Lower IC50 values (represented by darker blue) indicate higher potency. ( B ) Time-dependent response to extracts from T. melanoleuca and H. itama in U2932 and H1975 cell lines, as well as healthy PBMC. ( C ) H1975 and U2932 cell lines treated with osimertinib and doxorubicin.

    Journal: Scientific Reports

    Article Title: Anti-cancer activity of propolis extracts from stingless bees of Brunei Darussalam

    doi: 10.1038/s41598-025-32628-0

    Figure Lengend Snippet: Dose-dependent and time-dependent response of stingless bee ethanol extracts on cancer cell lines. ( A ) Heatmap of IC50 values across cell lines (EJ, H1975, U2932, HT, and OCI-LY3) and bee species ethanol extracts ( T. melanocephala , H. itama , L. canifrons , G. thoracica , and T. binghami ). Lower IC50 values (represented by darker blue) indicate higher potency. ( B ) Time-dependent response to extracts from T. melanoleuca and H. itama in U2932 and H1975 cell lines, as well as healthy PBMC. ( C ) H1975 and U2932 cell lines treated with osimertinib and doxorubicin.

    Article Snippet: DLBCL U2932 cell line (Catalog no. ACC 633, DSMZ, Germany) were maintained in modified RPMI supplemented with 10% fetal bovine serum, 1% L-glutamine, and 1% penicillin-streptomycin.

    Techniques:

    Pathway enrichment following treatment of propolis ethanol extracts. Dot plots showing enriched cancer hallmark pathways based on differentially expressed genes following treatment with propolis ethanol extracts from three stingless bee species— H. itama , T. binghami , and T. melanoleuca . Dot size corresponds to the gene ratio, while color intensity represents the significance of enrichment (adjusted p-value). Pathways are grouped by cell line, illustrating upregulated (up) and downregulated (down) expression patterns across treatments. ( A ) Significant results shown for EJ, H1975, and HT cell lines. ( B ) Significant results shown for U2932 cell line. ( C ) Western blot showing corroborative evidence for p53 pathway activation in H1975 cell line, and apoptosis induction in U2932 cell line.

    Journal: Scientific Reports

    Article Title: Anti-cancer activity of propolis extracts from stingless bees of Brunei Darussalam

    doi: 10.1038/s41598-025-32628-0

    Figure Lengend Snippet: Pathway enrichment following treatment of propolis ethanol extracts. Dot plots showing enriched cancer hallmark pathways based on differentially expressed genes following treatment with propolis ethanol extracts from three stingless bee species— H. itama , T. binghami , and T. melanoleuca . Dot size corresponds to the gene ratio, while color intensity represents the significance of enrichment (adjusted p-value). Pathways are grouped by cell line, illustrating upregulated (up) and downregulated (down) expression patterns across treatments. ( A ) Significant results shown for EJ, H1975, and HT cell lines. ( B ) Significant results shown for U2932 cell line. ( C ) Western blot showing corroborative evidence for p53 pathway activation in H1975 cell line, and apoptosis induction in U2932 cell line.

    Article Snippet: DLBCL U2932 cell line (Catalog no. ACC 633, DSMZ, Germany) were maintained in modified RPMI supplemented with 10% fetal bovine serum, 1% L-glutamine, and 1% penicillin-streptomycin.

    Techniques: Expressing, Western Blot, Activation Assay