Recombinant Heparinase I
Heparinase I – the ferment of lyase class, which catalyzes the break of glycosidic bond between N-sulphated hexosamine and 2-О-sulphated residue of iduronic and glucuronic acids, which leads to the cleavage of polysaccharide chain into oligosaccharide fragments. Heparinase I is highly active towards heparine and heparane sulphate and neutralizes their anti-coagulation activity.
Heparinase I developed by our company is a recombinant chimaeric polypeptide, comprised of heparinase I Pedobacter heparinus and stabilizing protein.
This ferment quickly and specifically neutralizes both un-fractionated and low-molecular heparin. The presence of the stabilizing protein provides unprecedented stability and significantly increased storage period in comparison with the competitors.
- Neutralization of heparine in blood and plasma samples before conducting coagulometry.
- Neutralization of low-molecular heparines in vitro.
- As a component of diagnostic tests for heparine neutralization.
- In glass-tubes for taking blood samples.
- Production of low-molecular heparine from the non-fractioned one.
- Reagent for research purposes (glycosaminoglycans’ degradation).