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Chloromethylketone-FPR, (FPRCK) (FITC)

Chloromethylketone-FPR, (FPRCK) (FITC)

Cat no: C5028

Supplier: United States Biological
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Tri-peptide chloromethylketones have been utilized extensively to irreversibly inhibit various serine proteases. Among the most common chloromethylketones are FPRCK (Phe-Pro-Arg-chloromethylketone), which is a rapid inhibitor of a-thrombin and EGRCK (Glu-Gly-Arg-chloromethylketone), which rapidly inhibits factor Xa. Recently, the modification of these tri-peptide chloromethylketones with reporting groups, such as fluorescent probes, radioactive labels or thioreactive-labels, has provided a unique approach to the study of various serine proteases. These probes are useful because they allow a means of reporting molecular changes in an enzyme, and not its zymogen, while also inhibiting the enzymatic activity. Applications: The fluorescein labelled compounds are useful in both Western Blot and fluorescent imaging applications. Other applications not tested. Recommended Dilutions: Optimal dilutions to be determined by the researcher. Special Properties: Tri-peptide chloromethyl ketones are very potent and irreversible inhibitors of serine proteases. BFPRCK is especially useful for inhibition of thrombin and tPA, while BEGRCK is useful for inhibition of factor Xa. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. .
Catalogue number: C5028
Applications: Immunofluorescence, Western Blot
Size: 1mg
Form: Supplied as a liquid in DMSO. Lebeled with Fluorescein isothiocyanate (FITC)
Purity: Fluorescein labelled FPRCK is prepared by the method of Williams et al. (11).
References: 1. Kettner, C. and Shaw, E., Methods Enzymol., 80, 826 (1981). 2. Ganu, V.S. and Shaw, E., Thromb. Res., 45, 1 (1987). 3. Kettner, C. and Shaw, E., Biochim. Biophys. Acta, 569, 31 (1979). 4. Kettner, C., et al., Arch. Biochem. Biophys., 202, 420 (1980). 5. Kettner, C. and Shaw, E., Bochemistry, 17, 4778 (1978). 6. Kettner, C. and Shaw, E., Thromb. Res., 22, 645 (1981). 7. Lollar, P. and Fass, D.H., Arch. Biochem. Biophys., 233, 438 (1984). 8. Boskovic, D.S., et al., J. Biol. Chem., 265, 10497 (1990). 9. Rauber, P., et al., Anal. Biochem., 168, 259 (1988). 10. Bock, P.E., Biochemistry, 27, 6633 (1988). 11. Williams, E.B., et al., J. Biol. Chem., 264, 7536, (1989). 12. Mann, K.G., et al., Blood, 76, 755 (1990). 13. Hartshorn, J.N., et al., Blood, 78, 833 (1991).

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