Description
Product Characteristics:
The caspase family of cysteine proteases play a key role in apoptosis. Caspase 3 is the most extensively studied apoptotic protein among caspase family members. Caspase 3 is synthesized as inactive pro enzyme that is processed in cells undergoing apoptosis by self proteolysis and/or cleavage by other upstream proteases (e.g. Caspases 8, 9 and 10). The processed form of Caspase 3 consists of large (17 kDa) and small (12 kDa) subunits which associate to form an active enzyme. Caspase 3 is cleaved at Asp28 Ser29 and Asp175 Ser176. The active Caspase 3 proteolytically cleaves and activates other caspases (e.g. Caspases 6, 7 and 9), as well as relevant targets in the cells (e.g. PARP and DFF). Alternative splicing of this gene results in two transcript variants which encode the same protein. In immunohistochemical studies Caspase 3 expression has been shown to be widespread but not present in all cell types (e.g. commonly reported in epithelial cells of skin, renal proximal tubules and collecting ducts). Differences in the level of Caspase 3 have been reported in cells of short lived nature (eg germinal centre B cells) and those that are long lived (eg mantle zone B cells). Caspase 3 is the predominant caspase involved in the cleavage of amyloid beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease.
Subcellular location: Cytoplasm
Synonyms: Caspase-3 subunit p12, APOPAIN, CASP3, Caspase 3 apoptosis related cysteine protease, Caspase3, CPP32, CPP32B, Cysteine protease CPP32, Human cysteine protease CPP32 isoform alpha mRNA complete cds, PARP cleavage protease, SCA 1, SCA1, SREBP cleavage activity 1, Yama, CASP3_HUMAN, Caspase-3, CASP-3, Apopain, Protein Yama, SREBP cleavage activity 1, SCA-1.
Target Information: This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq, Jul 2008]