Thrombin

Thrombin is an active enzyme in the earliest steps of the blood clot formation, generated from its circulating inactive precursor prothrombin. Thrombin is a glycoprotein formed by two peptides chains of 36 and 259 amino acids linked by disulfure bonds. Three important sites have been identified on the surface of the enzyme: The catalytic site that confers to the molecule its serine protease activity, the exosite one responsible for the binding of the substrate (fibrinogen or thrombin receptor) and the exosite two responsible for the binding of antithrombin III and inactivation of thrombin (1). The molecular mass of thrombin is 37kD.\n\nApplications: \nSuitable for use in ELISA and Western Blot. Other applications not tested.\n\nRecommended Dilution:\nELISA: 1:250\nOptimal dilutions to be determined by the researcher.\n\nHybridoma: \nX63-Ag8.653 myeloma cells with spleen cells from CF1xBalb/c mice.\n\nCulture Medium:\nDulbecco

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SPECIFICATIONS

Catalog Number

T5045-01D

Size

100ul

Applications

ELISA, WB

Hosts

Mouse

Reactivities

Hum

Form

Supplied as a liquid in PBS, pH 7.2, 15mM sodium azide, before the addition of glycerol to 40%.\n

P Type

Mab

Purity

Purified by Protein A/G affinity chromatography from culture supernatant.

Isotype

IgG1,k

References

1. Fenton JW 2nd, Bing DH Thrombin active-site regions. Sem Thromb Hemost 12:200-208. (1986). 2. Skrzypczak-Jankun eE,et al., Structure of the Hirugen and Hirolog 1 complexes of alfa-Thrombin. J.Mol.Biol. 221:1378-1393 (1991). 3. Rydel T J, Tulinsky A, Bode W, Huber R (1991) Refined structure of the Hirudin-Thrombin Complex J. Mol. Biol. 221: 283-601 (1991).

Additional Info

Recognizes human thrombin. Also recognizes complex of human thrombin with the thrombin inhibitor hirudin. No cross-reaction is seen with pro-thrombin. A strong reaction is seen in ELISA with thrombin directly coated onto the microtiterplate. Biotinylation of thrombin blocks antibody binding.