ICH-1
Nedd-2 Lyophilized solid. Recombinant, human caspase-2 expressed in E. coli as a single polypeptide chain. Subsequently undergoes spontaneous auto-processing to yield the native active enzyme. Useful for the study of enzyme regulation, cleavage of target substrates, and inhibitor screening. Cleavage sites are located at Asp316, Asp330, and possibly Asp152. MW: 12000 and 19000. Specific activity: ≥1500 units/mg protein. One unit is defined as the amount of enzyme that will cleave 1.0 nmol of Ac-VDVAD-pNA (Cat. No. 218820) per h at 37°C, pH 7.2. Purity: ≥90% by SDS-PAGE. M.W. 12,000 and 19,000 (heterodimer). Ref.: Talanian, R.V., et al. 1997. J. Biol. Chem. 272, 9677. Wang, L., et al. 1994. Cell 78, 739. |
