Active Rat Caspase-3

Caspase-3, rat recombinant
A cysteine-aspartic acid protease involved in apoptosis
Product Overview
Alternate Names / Synonyms: Active Rat Caspase-3, Caspase-3 Enzyme, caspase-3, rat caspase-3, rat caspases, active caspases, caspase-3 assay positive control
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Source: E. coli
Appearance: Lyophilized powder
Physical Form Description: Lyophilized powder
Molecular Weight: large (17 kD) and small (11 kD) subunits
Purity by SDS-PAGE: N/A
Purity by HPLC: N/A
Endotoxin Level: N/A
Biological Activity: 300,000 units/mg
Reconstitution Instructions: Reconstitute to 1 unit per µl in PBS containing 15% glycerol.
Storage Temp.: -70°C
Shipping: dry ice
Background Information: 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. 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 (Cat. #1008-200) or Ac-DEVD-AFC (1007-200).
Handling: Centrifuge the vial prior to opening.
Usage: For Research Use Only! Not to be used in humans.