|Calculated MW||large (20 kD) and small (10 kD) subunits.|
|Other Names||Caspase-1, Short name=CASP-1, Interleukin-1 beta convertase, Short name=IL-1BC, Interleukin-1 beta-converting enzyme, Short name=ICE, IL-1 beta-converting enzyme, p45|
|Application Notes||Reconstitute to 1 unit per µl in PBS containing 15% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Caspase-1 (also know as ICE) is a prototypical member of the caspase-family of cysteine proteases. Caspase-1 exists in cells as an inactive 45 kDa proenzyme. The pro-enzyme is matured by proteolysis to yield large (20 kD) and small (10 kD) subunits. The active caspase-1 is a heterotetramer consisting of two large and two small subunits. To date the regulatory mechanism of caspase-1 activation and the role of caspase-1 in apoptosis are poorly understood. In THP-1 cells, a large proportion of the caspase-1 is present in the inactive proenzyme form. The recombinant active mouse caspase-1 was expressed in E. coli. The active caspase-1 preferentially cleaves caspase-1 substrates (e.g., YVAD-AFC or YVAD-pNA) and is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-YVAD-pNA or Ac-YVAD-AFC
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