Cleaved Caspase-3 (Asp175), Cleaved Caspase-6 (Asp162), Cleaved Caspase-7 (Asp198), Cleaved Caspase-9 (Asp315), and Cleaved PARP (Asp214) Antibodies detect endogenous levels of the large cleavage fragments of their respective targets. Cleaved Caspase-9 (Asp330) Antibody detects the 37 kDa cleaved large fragment + prodomain and the 17 kDa large fragment. These antibodies will not cross-react with their respective full-length proteins.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to amino-terminal residues adjacent to Asp175 of human caspase-3 or to residues surrounding Asp214 in human PARP. Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to the amino-terminal residues adjacent to the proteolytic cleavage sites of human caspase-7, -9 or rat caspase-6. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
Description
The Cleaved Caspase Antibody Sampler Kit provides an economical means to evaluate the activation status of caspases by detecting their cleaved forms. The kit contains enough primary and secondary antibodies to perform four western blot experiments with each primary antibody.
Background
Apoptosis is a regulated physiological process leading to cell death. Caspases, a family of cysteine acid proteases, are central regulators of apoptosis. Initiator caspases (including 8, 9, 10 and 12) are closely coupled to proapoptotic signals. Once activated, these caspases cleave and activate downstream effector caspases (including 3, 6 and 7), which in turn cleave cytoskeletal and nuclear proteins like PARP, α-fodrin, DFF and lamin A, and induce apoptosis. Cytochrome c released from mitochondria is coupled to the activation of caspase-9, a key initiator caspase (1). Proapoptotic stimuli include the FasL, TNF-α, DNA damage and ER stress. Fas and TNFR activate caspases 8 and 10 (2), DNA damage leads to the activation of caspase-9 and ER stress leads to the calcium-mediated activation of caspase-12 (3). The inhibitor of apoptosis protein (IAP) family includes XIAP and survivin and functions by binding and inhibiting several caspases (4,5). Smac/Diablo, a mitochondrial protein, is released into the cytosol upon mitochondrial stress and competes with caspases for binding of IAPs. The interaction of Smac/Diablo with IAPs relieves the inhibitory effects of the IAPs on caspases (6).