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Caspase 9 (Cleaved Asp330) encodes 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 can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.
25 kDa caspase-9 dominant negative protein; APAF3; APAF-3; apoptotic protease activating factor 3; apoptotic protease MCH-6; Apoptotic protease-activating factor 3; CASP9; CASP-9; Casp9_v1; Casp-9-CTD; caspase 9; caspase 9, apoptosis-related cysteine peptidase; caspase-9; caspase-9 dominant negative form; Caspase-9 subunit p10; Caspase-9 subunit p35; caspase-9-carboxyl-terminal divergent; ICE-LAP6; ICE-like apoptotic protease 6; MCH6; PPP1R56; protein phosphatase 1, regulatory subunit 56
100 µL
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