资料参考

Caspase-1 (also know as Interleukin-1β-Converting Enzyme) is a prototypical member of the caspase-family of cysteine proteases. Caspase-1 exists in cells as an inactive 45 kDa proenzyme, which 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 mechanism of regulation of caspase-1 activation is complex and poorly understood. The recombinant active human caspase-1 was expressed in E. coli. The active caspase-1 preferentially cleaves caspase-1 substrates (YVAD-AFC or YVAD-pNA) and is routinely tested for its ability to enzymatically cleave Ac-YVAD-pNA or Ac-YVAD-AFC. The recombinant human Caspase-1 has an N-term His-tag and corresponds to amino acids 120-404 of Caspase-1. Active caspase-1 is useful in studying enzyme regulation, determining target substrates, screening caspase inhibitors, or as a positive control in caspase activity assays. We recommend using 1 unit/assay for analyzing caspase activity.