Caspase 8, active, Recombinant, Human (FLICE, MASH, Mch5)

Caspase-8 (also know as FLICE/MASH/Mch5) is a member of the interleukin-1b converting enzyme (ICE) family of cysteine proteases. Same as 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.\n\nThe 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).\n\nApplications:\nSuitable for use in Screening for caspase inhibitors, Studying enzyme regulation, Determining target substrates, and as Positive control in caspase activity assays. Other applications not tested.\n\nRecommended Usage:\nAnalyzing Caspase Activity: 1unit/assay.\nOptimum dilutions to be determined by the researcher.\n\nSpecific Activity: \n~5000units/mg\n\nUnit Definition: \nOne unit of the recombinant caspase-8 is the enzyme activity that cleaves 1nmol of the caspase substrate IETD-pNA (pNA: pnitroanaline) per hour at 37 degrees C in a reaction solution containing 50mM HEPES, pH 7.2, 50mM NaCl, 0.1% CHAPS, 10mM EDTA, 5% glycerol, 10mM DTT.\n\nStorage and Stability:\nLyophilized powder is stable for 1 year at -70 degrees C. Following reconstitution in PBS, the enzyme should be aliquoted and stored at -70 degrees C. Avoid multiple freeze/thaw cycles as activity might decrease.

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