Cleaved PARP (Asp214) (D64E10) XP®Rabbit mAb (Biotinylated) detects endogenous levels of the large fragment (89 kDa) of human PARP1 protein produced by caspase cleavage. The antibody does not recognize full length PARP1 or other PARP isoforms.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp214 in human PARP protein.
Description
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as unconjugated Cleaved PARP (Asp214) (D64E10) XP®Rabbit mAb #5625.
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 in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (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).
Storage: Supplied in 136 mM NaCl, 2.6 mM KCl, 12 mM
sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA and 50%
glycerol. Store at -20ºC. Do not aliquot antibody.