Caspase 8, recombinant human active

Caspase-8 is a member of the interleukin-1β converting enzyme (ICE) family of cysteine proteases. As with 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 form of caspase-8 consists of large and small subunits which associate to form the active enzyme. The active caspase-8 has been shown to be involved in the proteolysis of poly (ADP-ribose) polymerase (PARP), an enzyme that is involved in DNA repair and genomic maintenance.

The active recombinant human caspase-8 was expressed in E. coli. The expressed caspase-8 spontaneously undergoes autoprocessing to yield the subunits characteristic of the active enzyme. The recombinant caspase-8 preferentially cleaves the substrates consisting of consensus sequence IETD (e.g., IETD-AFC and IETD-pNA). The recombinant enzyme can also be used as a positive control in caspase assays or in determining the specificty of caspase substrates.Recommended usage: 0.5-1 unit for fluorometric caspase assays and 2-4 units for colorimetric caspase assays. Optimal working dilutions must be determined by end user.

Recommended usage: 0.5-1 unit for fluorometric caspase assays and 2-4 units for colorimetric caspase assays.

Optimal working dilutions must be determined by end user.

Lyophilized. Reconstitute with 25 μl PBS containing 15% glycerol.

Maintain at -70°C for 3-6 months. Avoid repeated freeze/thaw cycles.

Specific Activity: Where 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 37°C in a reaction solution containing 50 mM HEPES, 50 mM NaCl, 0.1% CHAPS, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.

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