||Recombinant Human CASP7 expressed inE.colispontaneously undergoes autoprocessing to yield the subunits characteristic of the active enzyme. The rate of caspase-7 enzymatic hydrolysis can be measured by the release of AMC from the caspase substrate Ac-DEVD-AMC as emission at 440nm and excitation at 380nm using a spectrofluorometer.
||Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing by upstream caspases (caspase-8, -9)at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms.
||Liquid. 5µg in 25µl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole.
||Stable at least one week when stored at +4°C. Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80°C.