Caspase Inhibitor Set III - Calbiochem

General description

A set of eight ready to use cell-permeable, irreversible inhibitors of various caspase-family proteases. Contains 25 µl (2 mM) each of Caspase-1 Inhibitor VI, Z-YVAD-FMK (Cat. No. 218746); Caspase-2 Inhibitor I, Z-VDVAD-FMK (Cat. No. 218744); Caspase-3 Inhibitor II, Z-DEVD-FMK (Cat. No. 264155); Caspase-5 Inhibitor I, Z-WEHD-FMK (Cat. No. 218753); Caspase-6 Inhibitor I, Z-VEID-FMK (Cat. No. 218757); Caspase-8 Inhibitor II, Z-IETD-FMK (Cat. No. 218759); Caspase-9 Inhibitor I, Z-LEHD-FMK (Cat. No. 218761); and Caspase Inhibitor I, Z-VAD-FMK (Cat. No. 627610). Supplied with a data sheet.

Apoptosis is a normal process in development and morphogenesis. Many cells can be activated to undergo apoptosis following the interaction of selected ligands with cell surface receptors. Receptor-mediated apoptosis involves the activation of caspases (cysteine-containing aspartate-specific proteases). A distinctive feature of caspases is the requirement of an aspartic acid residue in the substrate P₁ position.



Caspase inhibitors act by binding to the active site of caspases and form either a reversible or an irreversible linkage. Caspase inhibitor design includes a peptide recognition sequence attached to a functional group such as an aldehyde (CHO), chloromethylketone (CMK), fluoromethylketone (FMK), or fluoroacyloxymethylketone (FAOM). Caspase inhibitors with a CHO group are reversible and those with a CMK, FMK, or FAOM group are irreversible and cell-permeable. FMK exhibits slightly less reactivity than CMK and therefore is more specific for the enzyme being inhibited.

Biochem/physiol Actions

Cell permeable: yes

Primary Target
Caspase-1, caspase-2, caspase-3, caspase-4, caspase-5, caspase-6, caspase-7, caspase-8

Reversible: no

Warning

Toxicity: Irritant (B)

Physical form

Supplied as 2 mM in DMSO.

Other Notes

Humke, E.W., et al. 1998. J. Biol. Chem.273, 15702.
Datta, R., et al. 1997. J. Biol. Chem. 272, 1965.
Martin, L.M., et al. 1997. J. Biol. Chem. 272, 7421.
Takahashi, A., et al. 1997. Exp. Cell Res.231, 123.
Talanian, R.V., et al. 1997. J. Biol. Chem. 272, 9677.
Thornberry, N.A., et al. 1997. J. Biol. Chem. 272, 17907.
Nicholson, D.W., et al. 1995. Nature376, 37.
Thornberry, N.A., et al. 1992. Nature356, 768.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany