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Caspases, a family of endoproteases, are critical players in cell regulatory networks controlling inflammation and cell death. Initiator caspases (caspase-2, -8, -9, -10, -11, and -12) cleave and activate downstream effector caspases (caspase-3, -6, and -7), which in turn execute apoptosis by cleaving targeted cellular proteins. Caspase 3 plays a key role in the activation of sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Caspase 3 can form heterocomplex with other proteins. The cleaved fragment of Caspase 3 might form complex and shows at around 30-35 kDa by western blot (PMID: 25501826).
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Protein Aliases: Apopain; CASP-3; caspase 3, apoptosis-related cysteine peptidase; caspase 3, apoptosis-related cysteine protease; Caspase-3; CPP-32; Cysteine protease CPP32; PARP cleavage protease; procaspase3; Protein Yama; SCA-1; SREBP cleavage activity 1
Gene Aliases: CASP3; CPP32; CPP32B; SCA-1
UniProt ID: (Human) P42574
Entrez Gene ID: (Human) 836
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