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Recombinant Hirudin produced in Pichia. Pastoris contains 65 amino acid residues and having a molecular mass of 6979.5 Da.
rHirudin is fully biologically active when compared to standard. Its specific activity is ≥1×104ATU/mg.
Less than 10EU/mg of rhirudin as determined by LAL method.
>96% by SDS-PAGE and HPLC analyses.
This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C. Avoid repeated freeze/thaw cycles.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech Unlike heparin, hirudin act directly on thrombin, rather than through other clotting factors. They have a high binding affinity and specificity for thrombin. The mechanism of hirudin-thrombin binding appears to be unique. Recombinant hirudin variant is derived from yeast cell, the polypeptide containing 65 amino acid residues has a molecular weight of 6979.5 Da, which is identical to natural hirudin except for 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.