Recombinant Hirudin produced in Pichia. Pastoris contains 65 amino acid residues and having a molecular mass of 6979.5 Da.
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.
>96% by SDS-PAGE and HPLC analyses.
Lyophilized from a 0.2μm filtered solution of 20mM PBS, pH 7.0, containing 2% mannitol.
Sterile Filtered White lyophilized (freeze-dried) powder.
Yeast expression of a DNA sequence encoding the mature hirudin variant (Leu1,Thr2-63-desulfo hirudin).
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.
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 <-20oC. Further dilutions should be made in appropriate buffered solutions.
This lyophilized preparation is stable at 2-8oC, but should be kept at -20oC for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8oC. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20oC. Avoid repeated freeze/thaw cycles.