parp1 protein  (MedChemExpress)

Journal: Materials Today Bio

Article Title: Macrophage membrane coating enhances the therapeutic effects of Houttuynia cordata exosome-like nanovesicles against triple-negative breast cancer

doi: 10.1016/j.mtbio.2025.102604

Figure Lengend Snippet: MCELNs and CELNs elicited apoptosis in TNBC cells. (A)–(B) Flow cytometry detection of apoptosis in MDA-MB-231 cells treated with MCELNs and CELNs for 24 h. (C)–(D) Antagonism of MPA on cell apoptosis induced by MCELNs. (E)–(L) Western blot measured the expression levels of full length PARP1, cleaved PARP1, and cleaved caspase 3 following the treatment of MDA-MB-231 cells with MCELNs for 24 h ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Article Snippet: The main materials used in this study included P-CHK1, P-ATR, CDK4, CDC25C, P21, γ-H2AX (Abclone), cleaved PARP1, full length PARP1, cleaved caspase 3, BSA (BioFroxx), BCA Protein Concentration Assay Kit (Biyotime Shanghai), SDS-PAGE protein loading buffer (BOSTER, Wuhan), Three-color prestained protein standards (Abclone), Cell Cycle Assay Kit (RedFluorescence) (Biyotime Shanghai), enhanced RIPA lysate (BOSTER, Wuhan), RPMI 1640 medium(Gibco, USA), PKH67 (MedChemExpress, USA), PEG8000 (Chron Chemicals), 5-Fluorouracil (MedChemExpress, USA), and Camptothecin (MedChemExpress, USA).

Techniques: Flow Cytometry, Western Blot, Expressing

Journal: Materials Today Bio

Article Title: Macrophage membrane coating enhances the therapeutic effects of Houttuynia cordata exosome-like nanovesicles against triple-negative breast cancer

doi: 10.1016/j.mtbio.2025.102604

Figure Lengend Snippet: MCELNs and CELNs elicited apoptosis in TNBC cells. (A)–(B) Flow cytometry detection of apoptosis in MDA-MB-231 cells treated with MCELNs and CELNs for 24 h. (C)–(D) Antagonism of MPA on cell apoptosis induced by MCELNs. (E)–(L) Western blot measured the expression levels of full length PARP1, cleaved PARP1, and cleaved caspase 3 following the treatment of MDA-MB-231 cells with MCELNs for 24 h ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Article Snippet: The main materials used in this study included P-CHK1, P-ATR, CDK4, CDC25C, P21, γ-H2AX (Abclone), cleaved PARP1, full length PARP1, cleaved caspase 3, BSA (BioFroxx), BCA Protein Concentration Assay Kit (Biyotime Shanghai), SDS-PAGE protein loading buffer (BOSTER, Wuhan), Three-color prestained protein standards (Abclone), Cell Cycle Assay Kit (RedFluorescence) (Biyotime Shanghai), enhanced RIPA lysate (BOSTER, Wuhan), RPMI 1640 medium(Gibco, USA), PKH67 (MedChemExpress, USA), PEG8000 (Chron Chemicals), 5-Fluorouracil (MedChemExpress, USA), and Camptothecin (MedChemExpress, USA).

Techniques: Flow Cytometry, Western Blot, Expressing

Journal: Advanced Science

Article Title: Novel Cyano‐Artemisinin Dimer ZQJ29 Targets PARP1 to Induce Ferroptosis in Pancreatic Cancer Treatment

doi: 10.1002/advs.202501935

Figure Lengend Snippet: ZQJ29 inhibits PARP1 activity through direct binding with PARP1. A) PANC‐1 and KP4 cells were treated with varying concentrations of ZQJ29 for 24 h. B,C) Statistical analysis of Figure . D) PANC‐1 and KP4 cells were treated with 5 µM of ZQJ29 for specified periods. E,F) Statistical analysis of Figure . G) Molecular docking model illustrating the binding interaction between ZQJ29 and PARP1. H) Immunofluorescence staining of PARP1 (red) and nuclear DAPI staining (blue) in PANC‐1 and KP4 cells after 24 h treatment with ZQJ29 (0, 1, 2.5, and 5 µ m ). Scale bar: 200 µm. I) Thermal stability analysis of PARP1‐ZQJ29 interaction using CETSA across a temperature gradient (45‐70 °C). (J–K) Statistical analysis of Figure . L) PARP1 stability at 60 °C under treatment with different ZQJ29 concentrations. M,N) Statistical analysis of Figure . O) SPR assay. P) Stability of PARP1 treated with varying pronase/protein ratios. Q,R) Statistical analysis of Figure . S) PARP1 stability under different ZQJ29 concentrations (1:3000). T,U) Statistical analysis of Figure . The data was shown as mean value ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant.

Article Snippet: Recombinant human PARP1 protein (Sino Biological, 11040‐H08B) was immobilized on an activated carboxymethylated 5 (CM5) sensor chip using the amine coupling method.

Techniques: Activity Assay, Binding Assay, Immunofluorescence, Staining, SPR Assay

Journal: Advanced Science

Article Title: Novel Cyano‐Artemisinin Dimer ZQJ29 Targets PARP1 to Induce Ferroptosis in Pancreatic Cancer Treatment

doi: 10.1002/advs.202501935

Figure Lengend Snippet: ZQJ29‐induced ferroptosis is PARP1‐dependent. A) PPI network analysis. B) Protein expression in mouse tumor tissues. C) Statistical analysis of Figure . D) Heatmap of protein expression from proteomic data. E) Protein expression in PANC‐1 and KP4 cells treated with varying concentrations of ZQJ29. F,G) Statistical analysis of Figure . H–J) Protein expression in PANC‐1 and KP4 cells treated with ZQJ29 alone or in combination with PARP1 inhibitor (Olaparib), SLC7A11 inhibitor (Erastin), or GPX4 inhibitor (ML‐210). K–P) Statistical analysis of Figure . Q) Expression of PARP1, TP53, SLC7A11, and GPX4 in PANC‐1 and KP4 cells transfected with different PARP1 siRNAs. R,S) Statistical analysis of Figure Q. T,U) Cell viability assessed by CCK‐8 assay in PANC‐1 and KP4 cells transfected with control‐siRNA or PARP1‐siRNA, followed by treatment with ZQJ29 (1 µ m ) for 24 h. The data was shown as mean value ± SD. * p < 0.05; ** p < 0.01; *** p < 0.001; ns, not significant.

Article Snippet: Recombinant human PARP1 protein (Sino Biological, 11040‐H08B) was immobilized on an activated carboxymethylated 5 (CM5) sensor chip using the amine coupling method.

Techniques: Expressing, Transfection, CCK-8 Assay, Control

Journal: Advanced Science

Article Title: Novel Cyano‐Artemisinin Dimer ZQJ29 Targets PARP1 to Induce Ferroptosis in Pancreatic Cancer Treatment

doi: 10.1002/advs.202501935

Figure Lengend Snippet: The schematic illustration for ZQJ29 targeted PARP1 to activate ferroptosis for anti‐pancreatic cancer.

Article Snippet: Recombinant human PARP1 protein (Sino Biological, 11040‐H08B) was immobilized on an activated carboxymethylated 5 (CM5) sensor chip using the amine coupling method.

Techniques: