|Calculated MW||large (18 kDa) and small (11 kDa)|
|Other Names||Caspase-6, CASP-6, Apoptotic protease Mch-2|
|Application Notes||Reconstitute to 1 unit per µl in PBS containing 15% glycerol.|
|Storage||-70°C; Lyophilized powder|
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Provided below are standard protocols that you may find useful for product applications.
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 or Ac-VEID-AFC .
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Suzuki A.,et al.Oncogene 23:7067-7075(2004).
Burkard T.R.,et al.BMC Syst. Biol. 5:17-17(2011).
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