Caspase 1, recombinant human active

Caspase-1 (also known as ICE, Interleukin-1beta-Converting Enzyme) is the prototypical member of the caspase family of cysteine proteases. Caspase-1 exists in cells as an inactive 45 kDa pro-enzyme. The pro-enzyme is matured by proteolysis to yield large (20 kD) and small (10 kD) subunits. The active enzyme is a heterotetramer consisting of two large and two small subunits. To date the mechanism of regulation of caspase-1 activation is complex and poorly understood. In THP-1 cells, a large proportion of the caspase-1 is present in the inactive pro-enzyme form.

The active recombinant human caspase-1 was expressed in E. coli. The expressed caspase-1 spontaneously undergoes autoprocessing to yield the subunits characteristic of the native enzyme. The recombinant caspase-1 preferentially cleaves the substrates consisting of consensus sequence YVAD (e.g., YVAD-AFC and YVAD-pNA). The recombinant enzyme can also be used as a positive control in caspase assays or in determining the specificity 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.

Lyophilized. Reconstitute in 25 μL PBS containing 15% glycerol.

Maintain unopened and rehydrated product at -70°C in undiluted, freeze-thaw protected, tightly sealed aliquots. Avoid repeated freeze/thaw cycles. Product stable for 6 months from date of purchased if handled appropriately.

Partially purified recombinant caspase 3 with a full length HIS-6-tag. Approximately 10-20% caspase 1 protein. The remainder is E.Coli proteins. Approximately 0.8-2 mg total protein/U of activity; E.Coli proteins have no reactivity.

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