背景介绍 Selectivity for caspases-3 and 7 involves unique hydrophobic residues in the S2 pocket surrounding the catalytic cysteine residue. Sequence alignments of the active site residues of the caspases strongly suggest that the basis of this selectivity is due to binding in the S2 subsite comprised of residues Tyr204, Trp206, and Phe256 which are unique to caspases 3 and 7. In some systems inhibition of caspases-3 and -7 can prevent apoptosis and may therefore have important therapeutic implications. 产品介绍 A potent, cell-permeable, and specific, reversible inhibitor of caspase-3 and caspase-7.