Anti-human Caspase-3

Description: Caspases are present in all cells, recruitment of these proteases to oligomerized receptors leads to activation accompanied by autoproteolytic cleavage. Active caspases can proteolyze additional caspases generating a caspase cascade that cleaves proteins critical for cell survival. The final outcome of this signaling pathway is a form of controlled cell death termed apoptosis. The subgroup of caspases involved in apoptosis is called initiators or effectors. Caspase-3 cleaves substrate at the carboxyl terminus of aspartate residues. Active caspase-3 has two active sites and consists of two identical large (~ 20 kDa) and two identical small (~ 10 kDa) subunits that are derived from two precursor caspase-3 polypeptides. Caspase-3 is proteolytically activated by other caspases.

Both subunits contribute to substrate binding and catalysis. The active site cysteine that covalently binds the substrate is located near the C-terminus of the large subunit. Active caspase-3 has two-fold symmetry, two active site pockets each residing on an opposite side. Caspase-3, together with caspases 8 and 9, is situated at pivotal junctions in apoptotic pathways. Caspase-3 appears to amplify caspase 8 and 9 initiation signals into complete commitment to apoptotic disassembly.