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Conditions of optimal Hirudin Protein performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
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Introduction
Recombinant Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech unlike heparin. Hirudin acts directly on thrombin rather than through other clotting factors. The mechanism of Hirudin-thrombin appears to be unique. The conversion of fibrinogen into fibrin by the serine protease enzyme thrombin is a major event in the final stages of blood coagulation. In the final stages of coagulation prothrombinase converts prothrombin into thrombin. Fibrin is subsequently cross linked by factor XIII to form a blood clot. The primary inhibitor of thrombin in normal blood circulation is antithrombin III. The anticoagulatant activity of hirudin is derived from its ability to inhibit the pro-coagulant activity of thrombin (similar to antithrombin III activity). Hirudin is the strongest natural inhibitor of thrombin. Hirudin binds to and inhibits only the activity of thrombin forms with a specific activity on fibrinogen contrasting to antithrombin III activity. Therefore, hirudin has a thrombolytic activity since it prevents or dissolves the formation of clots and thrombi. Hirudin also has therapeutic significance in blood coagulation disorders, in the treatment of skin hematomas and of superficial varicose veins. Hirudin does not hinder with the biological activity of other serum proteins and can also act on complexed thrombin, thus having an advantage over more common anticoagulants and thrombolytics like heparin for example. It is complicated to extract large quantities of hirudin from natural sources; therefore a method for producing and purifying hirudin using recombinant biotechnology has been developed.
BP002436-PRO-362: Recombinant Hirudin protein
Source: Pichia Pastoris-derived.
Recombinant Hirudin protein is derived from yeast and the polypeptide chain contains 65 amino acids and its Mw is 6979.5 dalton which is identical to natural Hirudin except for the substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. The Recombinant Hirudin protein is purified by proprietary chromatographic techniques.
The biological activity of Recombinant Hirudin protein is measured using chromogenic assay, 1 unit is defined as the amount of Hirudin that neutralizes 1 unit of the WHO preparation 89/588 of thrombin. The specific activity of Recombinant Hirudin protein was found to be 16,000 ATU/mg protein.
Purity: > 95.0% by RP-HPLC and SDS-PAGE.
Formulation: Each mg of protein was lyophilized from a sterile solution containing no 20 mM PBS pH-7 and 2% mannitol.
Reconstitution: It is recommended to reconstitute the lyophilized Hirudin in sterile 18 M?-cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution.
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