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PARP-1 Antibody (Cleaved p85)

Rabbit Monoclonal Antibody

  • WB - PARP-1 Antibody (Cleaved p85) AJ1588b
    A. Western blot analysis on (1) Jurkat and (2) Jurkat + Camptothecin using anti-PARP-1 RabMAb (Cat. #AJ1588b), 1:1,000 dilution.
  • FC - PARP-1 Antibody (Cleaved p85) AJ1588b
    B. Flow cytometric analysis of apoptotic and non-apoptotic Jurkat cells using anti-cleaved PARP-1 RabMAb (Cat. #AJ1588b). Jurkat cells were either left untreated (A) or treated with camptothecin (4 uM, 5 hr) to induce apoptosis (B). Cells were fixed and permeabilized, and then stained with anti-cleaved PARP-1. The results indicate that 43% of cells were positive for cleaved PARP (B, M2) after treatment, compared to 9% positive without treatment (A, M2).
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P09874
Reactivity Human, Rat
Host Rabbit
Clonality Monoclonal
Clone Names Y34
Calculated MW 113084 Da
Gene ID 142
Other Names Poly [ADP-ribose] polymerase 1, PARP-1, ADP-ribosyltransferase diphtheria toxin-like 1, ARTD1, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1, PARP1, ADPRT, PPOL
Target/Specificity A synthetic peptide corresponding to residues following the cleavage site of human PARP-1 was used as immunogen. The antibody only recognize p85 cleaved-form of PARP-1.
Dilution WB~~1:1000~10000
Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPARP-1 Antibody (Cleaved p85) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name PARP1
Synonyms ADPRT, PPOL
Function Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.
Cellular Location Nucleus. Nucleus, nucleolus. Note=Localizes at sites of DNA damage
Research Areas
Citations (0)

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Poly (ADP-ribose) polymerase (PARP) is zinc-dependent DNA binding protein that recognizes DNA strand breaks and is presumed to play a role in DNA repair (1). As a marker for apoptosis, PARP is cleaved in vitro by many caspases, and in vivo by Caspase-3 (2,3). Existing as a 116 kDa nuclear protein, PARP is cleaved between amino acids Asp214 and Gly215 to yield two fragments of 29 kDa (C-terminal catalytic domain) and 85 kDa (N-terminal DNA-binding domain) (2,4).


1. Ikejima, M, et al. The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J.Biol.Chem. 265: 21907
2. Lazebnik, Y.A., et al. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371: 346
3. Tewari, M, et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801
4. Kaufmann, S.H., et al. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53: 2976

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Cat# AJ1588b
(40 western blots)
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