Caspase-3/7 Inhibitor I

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.

Store at or below –20°C. Solid form is stable at least 12 months from date of receipt, when stored as directed. Do not store aqueous solutions for more than one day.