Peptide-fluoromethyl ketone inhibitor of caspases 2 and 3. The FMK (fluoromethyl ketone, CH2F) inhibitor has several advantages over other types of derivatives: Penetrates cell membranes, is nontoxic to cells, irreversible inhibition.
Caspase-2 (also known as ICH-1) is a member of the caspase family of cysteine proteases involved in apoptosis. It is a member of the Group II caspases, along with caspase-3 and -7. Group II caspases prefer peptides of the DEXDtype as substrates. However, unlike caspase-3 and -7, caspase-2 requires a P5 amino acid in the peptide for efficient cleavage. The similar substrate specificities of the Group II caspases suggests that their roles in cells are at least overlapping, if not completely redundant. The requirement for a fifth amino acid in substrates for caspase-2 means that inhibitors of the DEVD-type, while inhibiting caspase-3 and -7, would have little effect on caspase-2 activity. For this reason, the Z-VDVAD-FMK inhibitor is excellent for studying the role of caspase-2 in apoptosis.
Specifically inhibits caspase-2 and to a lesser degree caspase-3. Also shows some inhibition of caspase-7.
Dissolve Caspase-2, -3 Inhibitor in high purity (>99.9%) DMSO before use.

For use on intact cells:
1. Prepare desired concentrated stock solutions as follows:
3 mg Z-VDVAD-FMK
in 43μl DMSO = 10 mM

2. Adding 2 μL of a 10 mM stock solution to 1 mL of culture medium gives a final Z-VDVAD- FMK concentration of 20 μM. Effective final concentrations are estimated to be 5-20 μM.