Caspase-7 Antibody detects endogenous levels of both full length caspase-7 (35 kDa) and the large fragment of cleaved caspase-7 following cleavage at aspartic acid 198 (20 kDa). The antibody does not recognize other caspases.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the cleavage site of human caspase-7. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis (2-4). Caspase-7 is an effector caspase (along with caspase-2 and -3), meaning that it cleaves essential cellular machinery rather than activating other caspases (5-8). Caspase-7 is cleaved by many enzymes, including caspases-3, -6, -8, -9 and granzyme B (1,4,5). Once activated, caspase-7 cleaves many of the same substrates as caspase-3, including poly (ADP-ribose) polymerase, or PARP (2,4).