资料参考

Caspase-3 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, caspase-8 and grazyme B. The active caspase-3 consists of large (17 kD) and small (11 kD) subunits. The active caspase-3 is involved in the proteolysis of poly (ADP-ribose) polymerase (PARP), the sterol regulatory element binding proteins (SREBPs), focal adhesion kinase (FAK), and others. Caspase-3 is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with Alzheimer's disease. The recombinant active human caspase-3 expressed in E. coli spontaneously undergoes autoprocessing to yield subunits characteristic of the native enzyme. The active caspase-3 preferentially cleaves caspase-3 substrates (DEVD-AFC or DEVD-pNA) and is routinely tested for its ability to enzymatically cleave Ac-DEVD-pNA or Ac-DEVD-AFC. Active caspase-3 is useful in studying enzyme regulation, determining target substrates, screening caspase inhibitors, or as a positive control in caspase activity assays. Recommend using 1 unit/assay for analyzing caspase activity.