Caspase-3, Human, Recombinant, E. coli

Toxicity: Standard Handling (A)

M.W. 12,000 and 17,000 (heterodimer).

Recombinant, human caspase-3 expressed in E. coli as the proenzyme, which is subsequently cleaved to produce the active enzyme. The active enzyme is a heterodimer with subunit molecular weights of 12 kDa and 19 kDa. Suitable for the study of enzyme regulation and kinetics, target substrate cleavage and inhibitor screening. Caspase-3 is a member of the ICE family of cysteine proteases that is activated during apoptotic signaling events by upstream proteases, including caspase-6, caspase-8 (FLICE) and cytotoxic T-cell-derived granzyme B.

Izban, K.F., et al. 1999. Am. J. Pathol. 154, 1439.
Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
Mittl, P.R.E., et al. 1997. J. Biol. Chem. 272, 6539.
Talanian, R.V., et al. 1997. J. Biol. Chem. 272, 9677.
Thornberry, N.A., et al. 1997. J. Biol. Chem. 272, 17907.

One unit is defined as the amount of enzyme that will cleave 1.0 pmol of the substrate Ac-DEVD-pNA (Cat. No. 235400) per min at 30°C, pH 7.4.

In 100 mM NaCl, 50 mM HEPES, 10 mM DTT, 1 mM EDTA, 10% glycerol, 0.5% CHAPS, pH 7.4.

Following initial thaw, aliquot and freeze (-70°C).

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