Thrombin, alpha, FPRCK, Bovine

Proteolytic Activation of Prothrombin: The serine protease a-thrombin is produced by proteolytic activation of the zymogen, prothrombin. The enzyme complex, prothrombinase, catalyzes the proteolysis of two peptide bonds in prothrombin, which gives rise to an NH2-terminal derived F1.2 region and the heterodimer, a-thrombin.\n

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SPECIFICATIONS

Catalog Number

T4039-10

Size

200ug

Form

Supplied as a liquid in 50% Glycerol/20mM Hepes, pH 7.4 and 150mM Sodium chloride.

Purity

Purified from prothrombin using a modification of the Lundblad procedure (1) as described by Nesheim, et al. (2). Purity is determined by SDS-PAGE analysis.

References

1. Lundblad, R.L., et al., Methods Enzymol. 45: 156 (1976). 2. Nesheim, M.E., et al., J. Biol. Chem., 258: 5386 (1983). 3. Fenton, J.W., et al., in Chemistry and Biology of Thrombin, ed. R.L. Lundblad, J.W. Fenton, K.G. Mann, pp. 43-70. Ann Arbor, MI: Ann Arbor Science Publishers, Inc., 1977. 4. Braughman, D.J., et al., J. Biol. Chem. 242: 5252 (1967). 5. Winzor, D.J., et al., Arch. Biochem. Biophys. 104: 202 (1964). 6. Fenton, J.W., et al., J. Biol. Chem. 252: 3587 (1977). 7. Winzor, D.J., et al., J. Phys. Chem. 68: 338 (1964). 8. Magnusson, S., in The Enzymes, ed. P.D. Boyer, vol. III, pp. 277-321. New York: Academic Press, 1971. 9. Gaun, K.L., Dixon, J.E., Anal. Biochem. 192: 262 (1991). 10. Germino, J., Bastia, D., PNAS USA 81: 4692 (1984). 11. Chang, J.-Y., Eur. J. Biochem. 151 217 (1985).

Additional Info

Specific Activity: ~3800 NIH u/mg\n(Activity is measured in a thrombin specific clotting assay and compared to standardized NIH thrombin).