Caspases are a family of cysteine proteases that centrally controls apoptotic machinery. Caspases can be grouped according to their substrate specificities that are largely determined by the amino acids preceding the cleavage site. One group of caspases that include -6, -8, is specific for the substrate V/LEXD. This substrate is a site similar to those found in caspase proenzymes. This group of caspases may function as initiators of a proteolytic cascade by activating pro-caspases to amplify a death signal. A second group of caspases is specific for the substrate DEXD that is related to sites found on target proteins cleaved during apoptosis.
Caspase-3 is a member of the interleukin-1 beta converting enzyme, Caspase-8, nuclear lamins and others. The overexpression of Caspase-3 can result in apoptosis. Likewise, the inhibition of Caspase-3 or other caspases can prevent cells from entering the apoptotic pathway. Recent evidence has revealed a link between plasma caspase-3 and atherosclerosis and it role in activation of apoptosis in breast cancer mediated by siRNA-mediated Apollon silencing. This antibody is specific for the cleaved (active) form of caspase-3.
Apopain; apoptosis-related cysteine protease; CASP-3; caspase 3; caspase 3, apoptosis related cysteine protease; caspase 3, apoptosis-related cysteine peptidase; caspase 3, apoptosis-related cysteine protease; Caspase-3; CPP-32; Cysteine protease CPP32; LICE; PARP cleavage protease; procaspase3; Protein Yama; SCA-1; SREBP cleavage activity 1; Yama
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