Description
Protocol
Available protocols: ELISA+
Specificity / Sensitivity
PathScan
Species Reactivity: Human, Monkey
Background
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases (2,3) and is one of the main cleavage targets of caspase-3 (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA-binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).
Alternate Names
ADP-ribosyltransferase (NAD+); ADP-ribosyltransferase diphtheria toxin-like 1; ADP-ribosyltransferase NAD(+); ADPRT; ADPRT 1; ADPRT1; ARTD1; DNA ADP-ribosyltransferase PARP1; NAD(+) ADP-ribosyltransferase 1; pADPRT-1; PARP; PARP-1; PARP1; poly (ADP-ribose) polymerase; poly (ADP-ribose) polymerase 1; poly (ADP-ribose) polymerase family, member 1; Poly [ADP-ribose] polymerase 1; poly(ADP-ribose) polymerase; poly(ADP-ribose) polymerase 1; poly(ADP-ribose) synthetase; poly(ADP-ribosyl)transferase; Poly[ADP-ribose] synthase 1; PPOL; Protein poly-ADP-ribosyltransferase PARP1
