form
solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
desiccated
shipped in
ambient
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
caspase-1, caspase-2, caspase-4, caspase-5, caspase-6, caspase-7, caspase-8, caspase-9
granzyme B
Disclaimer
General description
This product has been discontinued.
A set of eight cell-permeable, irreversible inhibitors of various caspase-family proteases. Contains 250 µg 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 III, Boc-D-FMK (Cat. No. 218745). Supplied with a data sheet.
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. FMK exhibits slightly less reactivity than CMK and therefore is more specific for the enzyme being inhibited.
Other Notes
Humke, E.W., et al. 1998. J. Biol. Chem.273, 15702.
Takahashi, A., et al. 1997. Exp. Cell Res.231, 123.
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.
Preparation Note
Desc. Field- added "A set of eight cell-permeable, irreversible inhibitors of various caspase-family proteases"
Legal Information
Storage Class
10-13 - German Storage Class 10 to 13
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