PARP-1 p116

GWB-5F98BB

A synthetic peptide corresponding to residues before the cleavage site of human PARP-1 was used as immunogen. The antibody only recognizes full-length form (p116) of PARP-1.

WB: 1:1 000IP: 1:80. Poly (ADP-ribose) polymerase (PARP) is zinc-dependent DNA binding protein that recognizes DNA strand breaks and is presumed to play a role in DNA repair (1). As a marker for apoptosis PARP is cleaved in vitro by many caspases and in vivo by Caspase-3 (2 3). Existing as a 116 kDa nuclear protein PARP is cleaved between amino acids Asp214 and Gly215 to yield two fragments of 29 kDa (C-terminal catalytic domain) and 85 kDa (N-terminal DNA-binding domain) (2 4). 1. Ikejima M et al. The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J. Biol. Chem. 265: 219072. Lazebnik Y. A. et al. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371: 3463. Tewari M et al. Yama/CPP32 beta a mammalian homolog of CED-3 is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 8014. Kaufmann S. H. et al. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53: 29765. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487