Rabbit anti parp 1

Manufactured by Santa Cruz Biotechnology

Sourced in Germany, United States

Rabbit anti-PARP-1 is a primary antibody that specifically recognizes the Poly(ADP-ribose) Polymerase 1 (PARP-1) protein. PARP-1 is a nuclear enzyme involved in various cellular processes, including DNA repair, genomic stability, and programmed cell death. This antibody can be used for the detection and analysis of PARP-1 in various experimental applications, such as Western blotting, immunohistochemistry, and immunoprecipitation.

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Close spelling variants of this product

PARP-1 (120 citations) Anti-PARP (71 citations) Anti-PARP-1 (65 citations) Rabbit anti-PARP (7 citations) Rabbit anti-TM (2 citations)

6 protocols using rabbit anti parp 1

Western Blot Analysis of Protein Expression

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For the analysis of protein expression, cell pellets were washed and resuspended in PBS. Cells were centrifuged and pellets were stored at −20 °C. Cell pellets were then lysed in Winman’s buffer containing 1% NP-40, 0.1 M Tris–HCl pH 8.0, 0.15 M NaCl, and 5 mM EDTA, complemented with protease inhibitor cocktail (Roche). The total protein content was quantified using the DC™ Protein Assay kit (Bio-Rad, Hercules, CA, USA) according to manufacturer’s instructions. Protein lysate (20 µg) were loaded on 12% SDS-PAGE gel and transferred into a nitrocellulose membrane (GE Healthcare, Cleveland, OH, USA). The following primary antibodies were used: rabbit anti-PARP-1 (1:2000, sc-7150, Santa Cruz Biotechnology, Heidelberg, Germany), mouse anti-Caspase 3 (1:2000, 05-654, Merck Millipore, Darmstadt, Germany), and goat anti-actin (1:2000, sc-1616, Santa Cruz Biotechnology). The corresponding secondary antibodies were: anti-rabbit IgG-HRP, anti-mouse IgG-HRP, or anti-goat IgG-HRP (1:2000, Santa Cruz Biotechnology). The Amersham™ ECL Western Blotting Detection Reagents (GE Healthcare), the High Performance Chemiluminescence Film (GE Healthcare), and the Kodak GBX developer and fixer (Sigma) were used for signal detection [35 (link),36 (link)].

Pereira J.M., Lopes-Rodrigues V., Xavier C.P., Lima M.J., Lima R.T., Ferreira I.C, & Vasconcelos M.H. (2016). An Aqueous Extract of Tuberaria lignosa Inhibits Cell Growth, Alters the Cell Cycle Profile, and Induces Apoptosis of NCI-H460 Tumor Cells. Molecules, 21(5), 595.

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Western Blot Analysis of DNA Damage Response

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Cells were lysed in 50 mM Tris pH 8.0, 150 mM NaCl, 0.5% NP‐40, 50 mM NaF, 1 mM Na₃VO₄, 1 mM PMSF, one tablet protease inhibitors (EDTA free, Roche) per 10 ml, and 30 μg/ml DNaseI (Sigma‐Aldrich) and analyzed by Western blot analysis. For detection of proteins by chemoluminescence (Advansta, K‐12049‐D50), a mouse anti‐CHK1 (CS 2360, 2G1D5), rabbit anti‐ɣH2A.X (CS 2577), rabbit anti‐p53 (Santa Cruz sc‐6243), rabbit anti‐PARP1 (CS 9542), mouse anti‐HSP90 (Santa Cruz sc‐13119), mouse anti‐CycD3 (BD 554195), mouse anti‐hBCL2 (clone S100), rabbit anti‐ATR‐pSer428 (CS 2853), or rabbit anti‐actin (CS 4967) was used. Goat anti‐rabbit Ig/HRP (Dako, P0448) or rabbit anti‐mouse Ig/HRP (Dako, P0161) was used as secondary reagent.

Schuler F., Afreen S., Manzl C., Häcker G., Erlacher M, & Villunger A. (2019). Checkpoint kinase 1 is essential for fetal and adult hematopoiesis. EMBO Reports, 20(8), e47026.

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Oncogenic KIT Mutant Protein Autophagy

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GIST430 and GIST48 cells encoding the exon 11^{V560_L576del (het)}/13^V654A and exon 11^V560D/17^D820A mutant KIT oncoprotein, respectively, were gifts from Dr. Jonathan Fletcher (Harvard Medical School, USA). AUY922 was kindly supplied by Novartis. Rapamycin, 3-MA, bafilomycin A₁, CelLytic^TM cell lysis reagent, and rabbit anti-MAP1LC3A/B were purchased from Sigma Aldrich. Primary antibodies against KIT and phospho-KIT (Tyr703) were obtained from DAKO and Invitrogen, respectively. Antibodies against RPS6KB1, phospho-RPS6KB1 (Thr389), MAPK1/3, phospho-MAPK1/3 (Tyr204/Thr202), AKT, phospho-AKT (Ser473), BECN1, and ATG5 were purchased from Cell Signaling Technology. Normal rabbit IgG, normal goat IgG, normal mouse IgG, goat anti-MAP1LC3B, rabbit anti-PARP1, and mouse anti-SQSTM1 were obtained from Santa Cruz Biotechnology. Antibodies against HSPA1A and ACTIN were obtained from Stressgen and Millipore, respectively.

Hsueh Y.S., Chang H.H., Chiang N.J., Yen C.C., Li C.F, & Chen L.T. (2014). MTOR inhibition enhances NVP-AUY922-induced autophagy-mediated KIT degradation and cytotoxicity in imatinib-resistant gastrointestinal stromal tumors. Oncotarget, 5(22), 11723-11736.

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Protein Detection via Immunoblotting

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The presence of various proteins in the samples was confirmed by 10 % SDS-PAGE, followed by electroblotting to PVDF membranes and detection using the respective primary antibodies: rabbit anti-p53 (SantaCruz, sc-6243, 1:1,500), rabbit anti-15-phosphoserine (SantaCruz, sc-101762, 1:2000), rabbit anti-Mekk1 (SantaCruz, sc-252, 1:1,500), mouse anti-β–tubulin (SantaCruz, sc-5286, 1:1,500), and rabbit anti-PARP-1 (SantaCruz, sc-74469, 1:1,500), mouse anti-β-actin (SantaCruz,, 1:10,000), and mouse anti-Mdm2 (SantaCruz, sc-965 1:2000). Alkaline phosphate-conjugated secondary anti-rabbit (Sigma, A8025) or anti-mouse (Sigma, A7434) antibodies were used at 1:10,000 dilution. Following equilibration in chemiluminescence buffer (0.1 M diethanolamine, 1 mM MgCl₂, pH 9.5) for 5 min, the membranes were incubated with substrate CDP-Star (Amersham) for 5 min and exposed to film (RPI). For re-probing, the blots were stripped of primary and secondary antibodies using 20 mM Tris-HCl, pH 6.8 containing 1% SDS and 100 mM 2-mercaptoethanol at 55°C for 45 min on a rotating wheel (20 rpm), followed by extensive washing with water and blocking with 5% non-fat dry milk for at least 2 h prior to incubating again with primary antibodies.

Chipps E., Protzman A., Muhi M.Z., Ando S., Calvet J.P, & Islam M.R. (2015). Nuclear Localization Signal and p53 Binding Site in MAP/ERK Kinase Kinase 1 (MEKK1). Journal of cellular biochemistry, 116(12), 2903-2914.

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Western Blot and Immunofluorescence Antibodies

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For western blot, the following antibodies were used: rabbit anti-Ago2 (Sigma) at 1∶1000, mouse anti-HA (16B12, Covance) at 1∶2000, mouse anti-Ubc9 (BD biosciences) at 1∶1000, mouse anti-tubulin (Sigma) at 1∶10 000, in house rabbit anti-SUMO1 at 1∶1000, mouse anti-RanBP2 (Santa Cruz) at 1∶400, rabbit anti-SAE2 (Abcam) at 1∶1000, mouse anti-Ago1 (Upstate) at 1∶1000, mouse anti-Vinculin (Abcam) at 1/1000, rabbit anti-PARP1 (Santa Cruz) at 1∶1000 and mouse anti-GFP (Sigma) at 1∶500. For immunofluorescence, antibodies used are the following: rabbit anti-Dcp2 (Sigma) at 1∶300, mouse anti-HA (16B12, Covance) at 1∶500, rabbit anti-Ago2 (Abcam) at 1∶300. DAPI was purchased from Invitrogen. Cycloheximide and NaAsO₂ solution were purchased from Sigma.

Sahin U., Lapaquette P., Andrieux A., Faure G, & Dejean A. (2014). Sumoylation of Human Argonaute 2 at Lysine-402 Regulates Its Stability. PLoS ONE, 9(7), e102957.

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Protein Extraction and Subcellular Fractionation

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Total proteins were extracted with RIPA lysis buffer (Beyotime) containing 1% proteinase inhibitors (Beyotime). The mitochondria isolation followed the instructions of the Cell Mitochondria Isolation Kit (Beyotime). Nuclear and cytoplasmic proteins were isolated using a Nuclear and Cytoplasmic Protein Extraction Kit (Beyotime). The protein concentrations were quantified using a BCA Protein Assay Kit (Beyotime). Equal amounts of protein samples were subjected to 10–12% SDS-PAGE separation and then transferred to the polyvinylidene difluoride membrane (Millipore, Boston, MA, USA). Subsequent procedures were performed as described previously [38] (link). The following antibodies were used: rabbit anti-PARP-1 (1: 500, Santa Cruz, CA, USA), rabbit anti-AIF (1:1000, Abcam), rabbit anti-LC-3 (1:1000, Sigma-Aldrich), rabbit anti-p62 (1:1000, Cell Signaling Technology, MA, USA), mouse anti-PAR (1:1000, Enzo Life Sciences), mouse anti-β-actin (1:5000, Abbkine), rabbit anti-COX Ⅳ (1:1000, Proteintech, Wuhan, China), mouse anti-Histone H3 (1:3000, Abbkine), HRP-conjugated secondary antibodies (1:5000, Abbkine). Protein bands were detected by enhanced chemiluminescence kit (Thermo, USA).

Jiang H.Y., Yang Y., Zhang Y.Y., Xie Z., Zhao X.Y., Sun Y, & Kong W.J. (2017). The dual role of poly(ADP-ribose) polymerase-1 in modulating parthanatos and autophagy under oxidative stress in rat cochlear marginal cells of the stria vascularis. Redox Biology, 14, 361-370.

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