Description | A830040C14Rik,Apopain,CASP-3,CASP3,CASP3,Casp3a,Caspase 3,Caspase 3,apoptosis-related cysteine peptidase,Caspase 3,apoptosis-related cysteine protease,Caspase 3,apoptosis-related cysteine protease a,Caspase-3 subunit p12,CC3,CPP-32,CPP32,CPP32B,Cysteine protease CPP32,EC 3.4.22.56,LICE,mldy,OTTHUMP00000165052,OTTHUMP00000165053,OTTHUMP00000165054,PARP cleavage protease,Procaspase3,Protein Yama,SCA 1,SCA-1,SREBP cleavage activity 1,Yama,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 (also named CPP32, SCA-1, and Apopain) proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at the beginning of apoptosis. 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 also form heterocomplex with other proteins and performs MW of 50-70 kDa. This antibody can recognize p17, p19 and p32 of Caspase 3. 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]. |