Caspase-6, human recombinant

Caspase-6 (also know as Mch2) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-6 also exists in cells as an inactive proenzyme. During apoptosis procaspase-6 is processed at aspartate residues by self-proteolysis and/or cleavage by another caspase. The processed active form of caspase-6 consists of large (18 kDa) and small (11 kDa) subunits which associate to form the active enzyme. Active caspase-6 has been shown involving in the proteolysis of PARP (poly ADP-ribose polymerase), an enzyme that is involved in DNA repair and henomic maintenance. The recombinant active human caspase-6 was expressed in E. coli. The active caspase-6 is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-VEID-pNA (Cat. #1070-200) or Ac-VEID-AFC (1069-200).