Caspase 3, Recombinant, rat, active (CPP-32, Apoptain, Yama, SCA-1)

Caspase 3 is a key member of the caspase family of proteases. Caspase-3 exists in cells as an inactive 32kD proenzyme. During apoptosis procaspase-3 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases, such as caspase 6,8 or 9. The processed form of caspase 3 consists of large (17kD) and small (11kD) subunits which associate to form the active enzyme. Active caspase 3 involves in the proteolysis of several important molecules, such as PARP, SREBPs, FAK, and others. Active recombinant caspase 3 is tested for its ability to enzymatically cleave the colorimetric substrate Ac- DEVD-pNA. \n\nApplication(s): Active rat caspase 3 expressed in E. coli spontaneously undergoes autoprocessing to yield subunits characteristic of the native enzyme. Active caspase 3 preferentially cleaves caspase 3 substrates (e.g., DEVD-AFC or DEVD-pNA). Useful in studying enzyme regulation, determining target substrate, screening caspase inhibitors, or as positive control in caspase activity assays. We recommend using 1 unit/assay for analyzing caspase activity.\n\nUnit Definition: One unit of the recombinant rat caspase-3 is the enzyme activity that cleaves 1 nmol of the caspase substrate DEVD-pNA per hour at 37 degrees C in a reaction solution containing 50mM Hepes, pH 7.2, 50mM sodium chloride, 0.1% Chaps, 10mM EDTA, 5% glycerol, 10mM DTT. \n\nSpecific Activity: 10 units/ug \n\nLyophilized caspase 3 is stable for 1 year at -70 degrees C. Following reconstitution in PBS, the enzyme should be aliquoted and stored at -70 degrees C. Avoid multiple freeze/thaw cycles as activity may decrease.

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