Regulatory Status Legend

Description

Members of the caspase family have key roles in inflammation and mammalian apoptosis. Caspase-8 (FLICE/MACH-1) is a 55 kDa cytosolic protein with homology to the CD95/Fas-associated signal transduction molecule, FADD, in addition to its homology with other caspases. Caspase-8 is activated early in apoptosis and is involved in the proteolysis and activation of pro-caspase-3. The upstream sequence of the site recognized by active caspase-8, IETD (Ile-Glu-Thr-Asp), is utilized as a basis for the highly specific caspase-8 substrate, Ac-IETD-AFC, and the caspase-8 inhibitor, Ac-IETD-CHO. Ac-IETD-CHO (502 Daltons) is a synthetic tetrapeptide inhibitor of caspase-8 and contains the amino acid sequence that is the target for caspase-8 mediated proteolysis. The tetrapeptide inhibitor can be used as a negative (blocking) control, in parallel with Ac-IETD-AFC, to study caspase-8 activity in apoptotic cell lysates.