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Z-FA-FMK (Ready-to-Use)

Cathepsin inhibitor
ALX-260-148-R100 100 µl 2mM Inquire for pricing
ALX-260-148-R020 20 µl 10mM Inquire for pricing
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Cell permeable negative control for FMK-labelled caspase inhibitors. Irreversible inhibitor of cathepsins B, L, and S, and likely cathepsin H, as well as cruzain and papain. Has been shown to inhibit effector, but not initiator, caspases in vitro, and suppress some forms of apoptosis. Has been used in vivo.

Product Details

Alternative Name:Z-Phe-Ala-FMK, FMK caspase inhibitors negative control
Formulation:Liquid. In DMSO.
Purity:≥95% (HPLC)
Shipping:Blue Ice
Long Term Storage:-20°C
Technical Info/Product Notes:We recommend a final concentration of 2µM for use in cell cultures. The optimal doses may vary for different cells and culture conditions.
Regulatory Status:RUO - Research Use Only

Product Literature References

Coordination of receptor tyrosine kinase signaling and interfacial tension dynamics drive radial intercalation and tube elongation: N. Neumann, et al.; Dev. Cell 45, 67 (2018), Abstract; Full Text

General Literature References

Z-FA-fmk inhibits effector caspases but not initiator caspases 8 and 10, and demonstrates that novel anticancer retinoid-related molecules induce apoptosis via the intrinsic pathway.: F. J. Lopez-Hernandez et al.; Mol. Cancer. Ther. 2, 255 (2003), Abstract;
Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-betaL a process initiated by the exocytosis of cathepsin B.: M. Guo et al. ; J. Biol. Chem. 277, 14829 (2002), Abstract;
The cathepsin B inhibitor z-FA.fmk inhibits cytokine production in macrophages stimulated by lipopolysaccharide.: P. Schotte et al.; J. Biol. Chem. 276, 21153 (2001), Abstract;
Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents.: J. Lotem & L. Sachs; PNAS 93, 12507 (1996), Abstract;
Peptidyl fluoromethyl ketones as inhibitors of cathepsin B. Implication for treatment of rheumatoid arthritis.: N. K. Ahmed et al.; Biochem. Pharmacol. 44, 1201 (1992), Abstract;
The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B.: D. Bromme et al.; Biochem. J. 264, 475 (1989), Abstract;
Cysteine proteinase activity in arthritic rat knee joints and the effects of a selective systemic inhibitor, Z-Phe-AlaCH2F.: C. J. Van Noorden et al.; J. Rheumatol. 15, 1525 (1988), Abstract;
Visualization of time-dependent inactivation of human tumor cathepsin B isozymes by a peptidyl fluoromethyl ketone using a fluorescent print technique.: R. E.Smith et al.; Anticancer Res. 8, 525 (1988), Abstract;
Inactivation of thiol proteases with peptidyl diazomethyl ketones.: E. Shaw & G. D. Green ; Methods. Enzymol. 80, 820 (1981), Abstract;

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