|Application ||WB, FC|
|Calculated MW||113084 Da|
|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.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain 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.|
|Precautions||PARP-1 Antibody (Cleaved p85) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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|
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Provided below are standard protocols that you may find useful for product applications.
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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