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Proteins > Poly [ADP-ribose] polymerase 1 (PARP-1)
Poly [ADP-ribose] polymerase 1 (PARP-1)
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UniProt Number:
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P09874
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Alternate Names:
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Cleaved PARP (Asp214), Cleaved PARP, PARP1, PARP, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1
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Structure and Function:
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PARP-1 is nuclear DNA repair enzyme as component of base excision repair complex. It transfers ADP-ribose units from NAD+ to variety of nuclear proteins involved in chromatin architecture and in DNA metabolism including topoisomerases, histones and PARP itself. This modification follows DNA damages and leads to DNA repair. In apoptosis, PARP-1 is cleaved by activated caspase-3 between Asp214 and Gly215, resulting in the formation of an N-terminal 24 kDa fragment containing most of the DNA binding domain and a C-terminal 89 kDa fragment containing the catalytic domain. The proteolysis of PARP-1 through this cleavage renders the enzyme inactive and this further facilitates apoptotic cell death. Thus the presence of 89 kDa PARP-1 fragment is considered to be an important biomarker of apoptosis. PARP-1 is also cleaved by Caspase-7, Granzyme A and Granzyme B.
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Disease Associations:
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n/a
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Monoclonal Antibodies
In-Cell ELISA Kits
Protein Quantitation Assays
Western Blot Cocktails
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Related Pathways:
Apoptosis
NAD+ NADH Cycling
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