Bovine Thrombin Polyclonal Antibody
Affinity’s Bovine Thrombin Polyclonal Antibody is the base level of our Bovine Thrombin antibody family. The purity of IgG is typically 90% and is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v). The titre is essentially the same as the starting antiserum and each vial typically contains the amount of IgG recovered from one milliliter of antiserum. This Bovine Thrombin Polyclonal Antibody is generally intended for use in applications such as immuno-precipitation, immuno-electrophoresis, immuno-depletion and activity neutralization assays.
Product Code: SABT-IG
Retail Product Size: 10mg vial
Host Animal: Sheep Anti-Human Bovine Thrombin Polyclonal Antibody
Species Cross Reactivity: View Chart
Product Datasheet: Bovine Thrombin Polyclonal Antibody - purified anti-bovine sheep IgG
Description of Thrombin
Thrombin (EC184.108.40.206, α-thrombin) is the product of proteolytic activation of the zymogen prothrombin. Human thrombin is a two-chain serine protease with a mass of 37 kDa. The active site is located within the heavy chain. Thrombin has a high specificity for certain arginine bonds in protein substrates. The primary substrate is fibrinogen which thrombin converts to fibrin through the cleavage of four arginyl-glycyl peptide bonds. Thrombin is also an important activator of platelets, factor XIII, Protein C and TAFI (Plasma procarboxypeptidase B). In a positive feedback mechanism, thrombin increases the rate of its own production by activation of factors VIII and V. The rate of thrombin production is subsequently limited indirectly through the activation of Protein C by thrombin, which then inactivates the activated cofactors VIII and V. The binding of thrombin to thrombomodulin on the cell surface dramatically alters thrombin’s specificity, increasing it’s activity toward Protein C and TAFI, and decreasing it’s activity toward fibrinogen and activating cofactors VIII and V. In plasma, thrombin activity is inhibited primarily by antithrombin and to a lesser extent heparin cofactor II. The rate of inhibition by both of these inhibitors is profoundly increased in the presence of optimal concentrations of heparin. Other physiological inhibitors of thrombin in the absence of heparin include α2-macroglobulin and α1-antitrypsin1-4.
Weitz J, Hudoba M, Massel D, Maranganore J, Hirsch J: Clot-bound
Mann KG; Prothrombin and Thrombin; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 184-199, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
Stubbs MT, Bode W; A Player of Many Parts: The Spotlight Falls on Thrombin’s Structure; Thrombosis Research 69, pp 1-58, 1993.
Downing MW, Bloom JW, Mann KG; Comparison of the Inhibition of Thrombin by Three Plasma Protease Inhibitors; Biochemistry 17, pp 2649-2653, 1978.