mouse monoclonal IgG2a; caspase-3 Antibody (E-8) is an IgG2a κ mouse monoclonal caspase-3 antibody (also designated CASP3 antibody or CPP32 antibody) that detects the caspase-3 protein of human origin by WB, IP, IF, IHC(P), FCM and ELISA. caspase-3 Antibody (E-8) is available as both the non-conjugated anti-caspase-3 antibody form, as well as multiple conjugated forms of anti-caspase-3 antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. Caspase-3, also known as apopain, SCA-1, Yama and CPP32, is an aspartate-specific cysteine protease that belongs to the ICE subfamily of caspases. Caspase-3 is expressed in cells as an inactive precursor from which the p17 and p11 subunits of the mature caspase-3 are proteolytically generated during apoptosis. The caspase-3 precursor is first cleaved at Asp175-Ser176 to produce the p11 subunit and the p20 peptide. Subsequently, the p20 peptide is cleaved at Asp28-Ser29 to generate the mature p17 subunit. The active caspase-3 enzyme is a heterodimer composed of two p17 and two p11 subunits. At the onset of apoptosis, caspase-3 proteolytically cleaves PARP at an Asp216-Gly217 bond. During the execution of the apoptotic cascade, activated caspase-3 releases SREBP from the membrane of the ER in a proteolytic reaction that is distinct from their normal sterol-dependent activation. Caspase-3 cleaves and activates SREBPs between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Caspase-3 also cleaves and activates caspase-6, -7 and -9. The human caspase-3 gene encodes a cytoplasmic protein that is highly expressed in lung, spleen, heart, liver, kidney and cells of the immune system.