The nuclear protein PARP-1, or poly (ADP-ribose) polymerase, functions as a DNA damage sensor and plays a role in various DNA repair pathways. It has recently been implicated in a variety of cellular functions, including transcriptional regulation. PARP is an enzyme that catalyzes the transfer of ADP-ribose units from NAD+ to a variety of nuclear proteins including topoisomerases, histones, and PARP itself. During apoptosis, caspase-3 cleaves PARP at a recognition site in its DNA-binding domain to form 24 kDa and 89 kDa fragments, and the presence of the 89 kDa PARP cleavage fragment is considered a marker of cells that have undergone apoptosis. The F21-852 monoclonal antibody reacts only with the 89 kDa fragment of human PARP-1 that is downstream of the caspase-3 cleavage site (Asp214). It does not react with intact human PARP-1. Cross-reactivity with other members of the PARP superfamily is unknown. Recognition of cleaved PARP in mouse cells has been demonstrated, and it may also cross-react with other species.
Anti-Human cleaved PARP (F21-852)-143Nd—50 Tests