The human Caspase-3 Instant ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human Caspase-3 in cell extracts.
Caspases are a family of aspartate-specific cysteine proteases that act in a step-wise signaling manner like kinases. 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 activesite cysteine that covalently binds the substrate is located near the Cterminus 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.
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|Наименование: Каспаза-3, 96.|