Bovine Thrombin Polyclonal Antibody – Affinity Purified
Affinity’s Bovine Thrombin Polyclonal Antibody – Affinity Purified is the highest level of our Bovine Thrombin antibody family. During the Antigen Affinity Purification process the IgG has had any non-specific immunoglobulin fraction eliminated which enriches the specificity of the remaining immunoglobulin towards the target antigen. The result is a very high-purity product with a substantially higher titre than whole or purified IgG. Our Bovine Thrombin Polyclonal Antibody – Affinity Purified is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v) and is intended for applications such as immunoblotting, immunostaining of cells and several types of immunoassays where the higher signal-to-noise ratio achieved with this enriched product is required.
Product Code: SABT-AP
Retail Product Size: 0.5mg vial
Host Animal: Sheep Anti-Bovine Thrombin Polyclonal Antibody – Affinity Purified
Species Cross Reactivity: View Chart
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.
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2. 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.
3. Stubbs MT, Bode W; A Player of Many Parts: The Spotlight Falls on Thrombin’s Structure; Thrombosis Research 69, pp 1-58, 1993.
4. Downing MW, Bloom JW, Mann KG; Comparison of the Inhibition of Thrombin by Three Plasma Protease Inhibitors; Biochemistry 17, pp 2649-2653, 1978.