PARP1 (human, recombinant)

ADP-ribose Transferase 1|ADPRT|NAD+ADP-ribosyltransferase 1|PARP1|PARP-1|Poly(ADP-ribose) Polymerase 1|Poly(ADP-ribosyl)transferase

Poly(ADP-ribose) polymerase 1 (PARP1) is an ADP-ribosylating enzyme that has roles in DNA repair, maintenance of genomic integrity, and transcriptional regulation.{52890,52891} It is composed of an N-terminal DNA-binding domain (DBD) that contains the nuclear localization signal (NLS) and three zinc fingers that mediate PARP1 self-assembly and activation, a central automodification domain, and a highly conserved C-terminal catalytic domain.{52890,52892} PARP1 is ubiquitously expressed and localizes to the nucleus where it is recruited to sites of DNA damage induced by a variety of cellular stressors, including genomic, oxidative, inflammatory, or metabolic stress.{52893,52890} Binding of PARP1 to DNA single- or double-strand breaks activates its poly(ADP)-ribosylation (PARylation) catalytic activity. PARP1 PARylates itself, increasing its activity and recruiting additional DNA repair proteins to sites of damaged DNA, as well as PARylates other proteins, including transcription factors, to facilitate DNA damage repair.{52893,52890} PARP1 is subject to additional PTMs, including phosphorylation, methylation, and acetylation, that regulate its catalytic and DNA-binding activities.{52894} Increased PARP1 levels have been found in tumors isolated from patients with a variety of cancers, including soft tissue sarcoma and ovarian or squamous cell carcinomas, and are associated with decreased survival. Cayman's PARP1 (human, recombinant) protein can be used for enzyme assay applications. This protein consists of 1,040 amino acids and has a calculated molecular weight of 139 kDa.

-80

-80

40 mM Tris, pH 8.0, with 110 mM sodium chloride, 2.2 mM potassium chloride, 0.5 mM glutathione, 3 mM DTT, and 20% glycerol

180

≥80% as determined by SDS-PAGE