PARP-1 is a nuclear enzyme that synthesizes ADP-ribose polymers from NAD+, specifically binds Zn2+ and DNA, and recognizes single-strand breaks in DNA. PARP1 has been used in a study to assess racial and tissue-specific cancer risk associated with polymorphism in the PARP1 gene. It has also been used in a study to investigate inhibitors of PARP-1 for potential cancer treatments.
Poly(ADP-ribose) polymerase 1 (PARP-1) is associated with the inflammation response during atherosclerosis.
PARP-1 is inactivated by cleavage into a 24kDA and 89kDA fragment by activated caspase-3 or caspase-7. This results in the decreased ability to repair DNA damage and an increase in apoptosis.
PARP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 354 amino acids (662-1014a.a.) and having a molecular mass of 39.6 kDa. PARP1 is purified by proprietary chromatographic techniques.
PARP1 takes part in the base excision repair pathway, by catalyzing the poly ADP-ribosyl of a restricted number of acceptor proteins involved in chromatin architecture and in DNA metabolism.. PARP1 mediates the poly ADP-ribosy of APLF and CHFR. PARP1 positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. PARP1 is a chromatin-associated enzyme, poly (ADP-ribosyl) transferase, which modifies various nuclear proteins by poly ADP-ribosyl. PARP1 takes part in the regulation of various significant cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. PARP1 is a site of mutation in Fanconi anemia, and is involved in the pathophysiology of type I diabetes.
