Cleaved Caspase-9 (Asp353) Antibody (Rat Specific) detects endogenous levels of the large fragment (17 kDa or 38 kDa with prodomain) of caspase-9 resulting from cleavage at aspartic acid 353. The antibody does not recognize full length caspase-9 or any other cleaved caspases.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues surrounding Asp353 of rat caspase-9. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Caspase-9 (ICE-LAP6, Mch6) is an important member of the cysteine aspartic acid protease (caspase) family (1,2). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with the 47 kDa procaspase-9/Apaf 1. Apaf-1 mediated activation of caspase-9 involves instrinsic proteolytic processing resulting in cleavage at Asp315 and producing a p35 subunit. Additional cleavage occurs at Asp330 producing a p37 subunit that can serve to amplify the apoptotic response (3-6). Cleaved caspase-9 further processes other caspase members, including caspase-3 and caspase-7, to initiate a caspase cascade, which leads to apoptosis (7-10).