Caspase-1, human recombinant

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 human 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 (Cat. #1104-200) or Ac-YVAD-AFC (1103-200). The rh-Caspase has an N-term His-tag and corresponds to amino acids 120-404 of Caspase-1, gene accession# NP_150634.1.