|Calculated MW||large (17 kD) and small (11 kD) subunits|
|Other Names||Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1|
|Application Notes||Reconstitute in PBS containing 15% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Caspase-3 (also know as CPP32, Yama and apopain) is a major member of the caspase-family of cysteine proteases. Caspase-3 exists in cells as an inactive 32 kDa proenzyme. During apoptosis procaspase-3 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases, such as caspase-6 (Mch2), caspase-8 (Flice) and grazyme B. The processed form of caspase-3 consists of large (17 kD) and small (11 kD) subunits which associate to form the active enzyme. The active caspase-3 has been shown involving in the proteolysis of several important molecules, such as poly (ADP-ribose) polymerase (PARP), the sterol regulatory element binding proteins (SREBPs), focal adhesion kinase (FAK), and others. The recombinant active human caspase-3 expressed in E. coli spontaneously undergoes autoprocessing to yield subunits characteristic of the native enzyme (Full length gene Accession No. NP_004337) . The active caspase-3 preferentially cleaves caspase-3 substrates (e.g., DEVD-AFC or DEVD-pNA) and is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-DEVD-pNA or Ac-DEVD-AFC
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Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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