|Western blotting, Immunocytochemistry, In-Cell ELISA|
Host Species and Isotype:
|Mouse IgG1, κ|
Specific for Poly [ADP-ribose] polymerase 1 (cleaved)
This PARP-1 (cleaved) antibody reacts with the N-terminal end formed by the cleavage adjacent to Asp214. It recognizes the apoptosis-specific 89 kDa catalytic domain fragment, but it does not recognize the full-length PARP-1 or the 24 kDa DNA binding domain fragment.
PARP-1 is a nuclear DNA repair enzyme; it is a component of the base excision repair complex. PARP-1 transfers ADP-ribose units from NAD+ to a variety of nuclear proteins involved in chromatin architecture and in DNA metabolism including topoisomerases, histones, and PARP-1 itself. This modification follows DNA damage and leads to DNA repair. During apoptosis, PARP-1 is cleaved between Asp214 and Gly215 by activated caspase-3 resulting in the formation of an N-terminal 24 kDa fragment containing most of the DNA-binding domain and a C-terminal 89 kDa fragment containing the catalytic domain. The proteolysis of PARP-1 through this cleavage renders the enzyme inactive and further facilitates apoptotic cell death; therefore, the presence of the 89 kDa PARP-1 fragment is considered to be an important biomarker of apoptosis. PARP-1 is also cleaved by Caspase-7, Granzyme A, and Granzyme B.
For research use only. Not intended for any animal or human therapeutic or diagnostic use.