Description
Caspase-8 (also known as FLICE/MASH/Mch5) is a member of the interleukin-1b converting enzyme (ICE) family of cysteine proteases. Like other caspases, caspase-8 also exists in cells as an inactive proenzyme. During apoptosis pro-caspase-8 is processed at aspartate residues by self-proteolysis and/or cleavage by another caspase. The processed form of caspase-8 consists of large and small subunits which associate to form the active enzyme. The active recombinant human caspase-8 is routinely tested for its ability to enzymatically cleave the caspase-8 colorimetric substrate Ac-IETD-pNA.
<br.The E. coli expressed human caspase-8 spontaneously undergoes autoprocessing to form active caspase-8. The active caspase-8 efficiently cleaves substrates consisting of consensus sequence IETD (e.g., IETD-AFC and IETD-pNA)