Protein activity determined to be > 5000 units/mg. One unit of the recombinant caspase-8 is the enzyme activity that cleaves 1 nmol of the caspase substrate IETD-pNA (pNA: pnitroanaline) per hour at 37ºC in a reaction solution containing 50 mM Hepes, pH 7.2, 50 mM NaCl, 0.1% Chaps, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.
Reconstitute to 1 unit per μl in PBS containing 15% glycerol. Store at -80ºC.
Purity was assessed by SDS-PAGE (≥95%) and by HPLC.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Caspase-8, Caspase8, CASP8, ALPS2B, CAP4, Casp-8, FLICE, FLJ17672, MACH, MCH5, MGC78473, Casp 8, Caspase 8
Caspase-8 (also know as FLICE, MASH, Mch5) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-8 also exists in cells as an inactive proenzyme. During apoptosis procaspase-8 is processed at aspartate residues by self-proteolysis and/or cleavage by another caspase. The processed active form of caspase-8 consists of large and small subunits which associate to form the active enzyme. Active caspase-8 has been shown to activate caspase-3 leading to degradation of a variety of cellular target proteins during apoptosis. The recombinant active human caspase-8 was expressed in E. coli. The active caspase-8 is routinely tested at GeneTex for its ability to enzymatically cleave these two substrates Ac-IETD-pNA or Ac-IETD-AFC.