|Application ||WB, IHC|
|Calculated MW||113084 Da|
|Other Names||PARP1, ADPRT, PPOL, NAD(+) ADP-ribosyltransferase 1|
|Formulation||100 µg (0.2 mg/ml) affinity purified rabbit polyclonal anti-cleaved PARP antibody in phosphate-buffered saline (PBS) containing 50% glycerol, 1% BSA, and 0.02% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Precautions||PARP (Cleaved) Antibody 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 (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272). Mediates the poly(ADP-ribosyl)ation of APLF and CHFR (PubMed:17396150). 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 (PubMed:17177976). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). Mediates the poly(ADP-ribosyl)ation of histones in a HPF1-dependent manner (PubMed:27067600). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257).|
|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.
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, is a highly conserved nuclear enzyme implicated in DNA repair and in the apoptosis response of cells. This protein can be cleaved by many caspases in vitro and is one of the main cleavage targets of caspase-3 in vivo. The cleavage occurs between ASP214 and Gly 215, which separates PARP’s N-terminal DNA binding domain (24 kDa) from its C-terminal catalytic domain (89 kDa). It has been shown that cleavage of PARP facilitates cellular disassembly and inhibition of PARP cleavage attenuates apoptosis in vitro.
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