PAR/pADPr Antibody Best Seller

Detection of PAR/pADPr by Western Blot

PARP1 promotes PARP2 recruitment at DNA damage sites and niraparib enhances PARP2 foci independent of PARP1. (A) Representative images of laser-induced GFP-PARP2 and mRFP-XRCC1 foci in WT, Parp1 KO, Parp2 KO, and Parp1/2 DKO iMEF cells. The yellow arrowheads point to the area of micro-irradiation. (B) The relative intensity kinetics and (C) The normalized kinetics (plotted as the percentage of the maximal relative intensity at 1 min) of GFP-PARP2 at DNA damage sites in WT, Parp1 KO, Parp2 KO and Parp1/2 DKO iMEF cells. (D, E) The relative intensity of (B) GFP-PARP2 and (C) RFP-XRCC1 at 1 min post-microirradiation. Two-tailed unpaired Student's t-test were used to calculate the p-values. (F) Soluble and chromatin fraction of WT or PARP1 KO RPE-1 cells treated with MMS (0.1 mg/ml, 1 h) and niraparib (1 μM, 1 h). (G) The niraparib sensitivity of WT, PARP1 KO, PARP2 KO, and PARP1/2 DKO RPE-1 cells. The dots and error bars represent means and SEM, respectively, from one representative experiment out of three consistent biological repeats with triplicate samples (for sensitivity) and at least 8–10 cells (for live cell imaging) per experiment. P value of IC50 was calculated using the extra sum-of-square F test. ns, P > 0.05; **P < 0.01; ***P < 0.001. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35349716), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of PAR/pADPr by Western Blot

180055 blocks the catalytic activity of PARP1.A–C T47D (A), MDA-MB-231 (B), and MOLT4 cells (C) were pre-treated with Rucaparib or 180055 (1 μM) for 24 h and then challenged with H2O2 (2 mM) for 1 h. NAD+ levels were then determined; values represent mean ± SEM (n = 3 biological independent samples). Statistical significance was calculated with one-way ANOVA comparing the H2O2-treated DMSO group to the Rucaparib and 180055 groups. ***p < 0.001, ****p < 0.0001. D–F immunoblot analysis of PARylation levels in T47D (D), MDA-MB-231 (E), and MOLT4 cells (F) treated with either Rucaparib or 180055. Cells were pre-treated with a PARG inhibitor (PDD 00017273, 2 μM) for 1 h and then treated with Rucaparib or 180055 (1 μM) for 1 h. Cells were then challenged with H2O2 (2 mM) for 5 min, and whole cell lysates were analyzed using immunoblot assays with the indicated antibodies. Image collected and cropped by CiteAb from the following open publication (https://www.nature.com/articles/s41419-024-07277-2), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of PAR/pADPr by Western Blot

180055 blocks the catalytic activity of PARP1.A–C T47D (A), MDA-MB-231 (B), and MOLT4 cells (C) were pre-treated with Rucaparib or 180055 (1 μM) for 24 h and then challenged with H2O2 (2 mM) for 1 h. NAD+ levels were then determined; values represent mean ± SEM (n = 3 biological independent samples). Statistical significance was calculated with one-way ANOVA comparing the H2O2-treated DMSO group to the Rucaparib and 180055 groups. ***p < 0.001, ****p < 0.0001. D–F immunoblot analysis of PARylation levels in T47D (D), MDA-MB-231 (E), and MOLT4 cells (F) treated with either Rucaparib or 180055. Cells were pre-treated with a PARG inhibitor (PDD 00017273, 2 μM) for 1 h and then treated with Rucaparib or 180055 (1 μM) for 1 h. Cells were then challenged with H2O2 (2 mM) for 5 min, and whole cell lysates were analyzed using immunoblot assays with the indicated antibodies. Image collected and cropped by CiteAb from the following open publication (https://www.nature.com/articles/s41419-024-07277-2), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of Mouse PAR/pADPr by Western Blot

Regulation of NAD+-consuming enzymes PARP1 and PAR-AIF by Ginsenoside Rb1 in OGD/R-injured ASs. (A,B) Western blot analysis and quantification of PARP1 protein levels. (C,D) Western blot analysis and quantification of PAR. The band intensity of each protein was plotted after normalizing to the beta-tubulin signal of the same lane. Data are shown with mean ± SD, n = 3. ##p < 0.01 vs. Control group, * p < 0.05, ** p < 0.01 vs. OGD/R group based on one-way ANOVA with Fisher’s LSD test. (E,F) Immunofluorescence shows PAR expression in ASs. PAR (green—FITC) and nuclei stained by DAPI are shown, as well as the merged images. The bar graphs (mean ± SD, n = 5) represent the quantitative results of fluorescence intensity in 3 different fields for each group. (G,H) Immunofluorescence shows the distribution of AIF to the nucleus. AIF (green—FITC) and nucleus stained by DAPI are shown, as well as the merged images. Co-immunofluorescence analysis revealed that the nuclear translocation of AIF in OGD/R-injured ASs was blocked by Rb1 treatment. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/38003249), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of PAR/pADPr by Western Blot

180055 blocks the catalytic activity of PARP1.A–C T47D (A), MDA-MB-231 (B), and MOLT4 cells (C) were pre-treated with Rucaparib or 180055 (1 μM) for 24 h and then challenged with H2O2 (2 mM) for 1 h. NAD+ levels were then determined; values represent mean ± SEM (n = 3 biological independent samples). Statistical significance was calculated with one-way ANOVA comparing the H2O2-treated DMSO group to the Rucaparib and 180055 groups. ***p < 0.001, ****p < 0.0001. D–F immunoblot analysis of PARylation levels in T47D (D), MDA-MB-231 (E), and MOLT4 cells (F) treated with either Rucaparib or 180055. Cells were pre-treated with a PARG inhibitor (PDD 00017273, 2 μM) for 1 h and then treated with Rucaparib or 180055 (1 μM) for 1 h. Cells were then challenged with H2O2 (2 mM) for 5 min, and whole cell lysates were analyzed using immunoblot assays with the indicated antibodies. Image collected and cropped by CiteAb from the following open publication (https://www.nature.com/articles/s41419-024-07277-2), licensed under a CC-BY license. Not internally tested by R&D Systems.