Caspase 10 peptide

Caspases are a family of intracellular proteases that mediate cell death and are the principal effectors of apoptosis. Caspase 1 (Mch4, ICE-LAP4, FLICE2) plays an important role in apoptosis induced by a variety of inducers such as TNF alpha and Anti-Fas antibody. It is a large prodomain caspase classified together with caspases 2, 8, and 9 as a signaling caspase. Four isoforms of caspase 1 (caspase 1a, 1b, 1c, and 1d) having the same prodomain but different mature large and small subdomain, have been described. Caspase 1 contains two death domains (DED) involved in linking to the death effector domain of the adapter protein FADD and recruiting the complex to TNFR1 and Fas. The inactive procaspase 1 is variably expressed in many tissues and cell lines as a cytosolic protein. The mature form of caspase 1 comprises two subunits, p23/p17 (splice isoforms) and p12. Interestingly, a caspase 9- dependent processing of caspase 1 by caspase 6 in cell-free extracts has recently been suggested. Caspase 1 can cleave and activate caspases 3, 4, 6, 7, 8, and 9. This is followed by cleavage of numerous key proteins, including the nuclear protein PARP.