0.01M PBS pH7.4, 1% bovine serum albumin, 15 mM sodium azide
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
synthetic peptide corresponding to amino acid residues 359-372 of human caspase 10a p23/p17 with N-terminal added lysine conjugated to KLH with glutaraldehyde.
Purified by affinity chromatography
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Caspases are a family of intracellular proteases that mediate cell death and are the principal effectors of apoptosis. Caspase 10 (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 10 (caspase 10a, 10b, 10c, and 10d) having the same prodomain but different mature large and small subdomain, have been described. Caspase 10 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 10 is variably expressed in many tissues and cell lines as a cytosolic protein. The mature form of caspase 10 comprises two subunits, p23/p17 (splice isoforms) and p12. Interestingly, a caspase 9- dependent processing of caspase 10 by caspase 6 in cell-free extracts has recently been suggested. Caspase 10 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.