| Full Name | poly (ADP-ribose) polymerase 1 |
| Background | PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, is a highly conserved nuclear enzyme implicated in DNA repair and in the apoptosis response of cells. This protein can be cleaved by many caspases in vitro and is one of the main cleavage targets of caspase-3 in vivo. The cleavage occurs between ASP214 and Gly 215, which separates PARPs N-terminal DNA binding domain (24 kDa) from its C-terminal catalytic domain (89 kDa). It has been shown that cleavage of PARP facilitates cellular disassembly and inhibition of PARP cleavage attenuates apoptosis in vitro. |
| Synonyms | 142, pADPRT1, PARP-1, PARP cleaved, PARP, pADPRT-1, P09874, ADPRT1, PARP1, 173870, ADPRT, PPOL, PARP 1, pADPRT 1 |
| Cellular Localization | Nuclear |
| Specificity | This antibody specifically recognizes the 85 kDa fragment of cleaved PARP and can be used as a marker for detecting apoptotic cells. |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Immunogen | Synthetic peptide (Human) corresponding to N-terminus of cleavage site (214/215) of human PARP. |
| Antigen Species | Human |
| Species Reactivity | Human, Bovine |
| Conjugation | FITC |