|Calculated MW||two large (18 kDa) and two small (11 kDa) subunits in a heterotetramer form.|
|Other Names||Caspase-10, CASP-10, Apoptotic protease Mch-4, FAS-associated death domain protein interleukin-1B-converting enzyme 2, FLICE2, ICE-like apoptotic protease 4|
|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-10/a (also known as Mch4) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-10 also exists in cells as an inactive proenzyme. During apoptosis procaspase-10 is processed at aspartate residues to form active caspase-10 which consists of two large (18 kDa) and two small (11 kDa) subunits in a heterotetramer form. The recombinant active human caspase-10 was expressed in E. coli. The active caspase-10 is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-IETD-pNA or Ac-IETD-AFC
Fernandes-Alnemri T.,et al.Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
Vincenz C.,et al.J. Biol. Chem. 272:6578-6583(1997).
Ng P.W.,et al.J. Biol. Chem. 274:10301-10308(1999).
Hadano S.,et al.Genomics 71:200-213(2001).
Vonarbourg C.,et al.Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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