Caspase 10 human

Caspase 10 has two death effector domains (DEDs) that bind to the DED in the adapter molecule FADD and recruits both TNFR1 and CD95 to form complexes with these receptors. Caspase 10 cleaves and activates caspases 3, 4, 6, 7, 8 and 9 which causes the proteolytic cleavage of many key proteins such as PARP. Based on gene expression studies, caspase 10 may be crucial in embryonic development. In view of its structural homology to caspase 8, the initiator caspase in death receptor-mediated apoptosis, caspase 10 may function in a similar and redundant manner.

Lyophilized powder containing 0.052% ammonium sulfate, 0.158% Tris−HCl, and 0.76% sodium chloride.

One unit will hydrolyze 1 nmol of the caspase substrate IETD-pNA to IETD and p-nitroaniline per hour at pH 7.2 at 37 °C.