Heparinase I

heparinase iHeparinase I, also known as Heparin Lyase I, is endolytically and exolytically active on both heparin and highly sulfated domains of heparan sulfate. It cleaves selectively, via an elimination mechanism, highly sulfated polysaccharide chains containing 1-4 linkages between hexosamines and o-sulfated iduronic acid residues. The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. The enzyme also cleaves the antithrombin III binding pentasaccharide domain in the heparin molecule.

Recombinant enzyme homologous to its native counterpart and expressed in the natural host, Pedobacter heparinus (formerly, Flavobacterium heparinum).

  • Heparinase I is O-glycosylated at Ser-39.
  • EC Number: 4.2.2.7
  • Purity: ≥ 95 % by reversed phase HPLC analysis.
  • IBEX liquid heparinase I has optimal activity and stability for up to three years when stored frozen at -70°C.
  • IBEX lyophilized heparinase I has optimal activity and stability for up to two years when stored at 2-8oC .
  • Calcium dependent enzyme and has optimal activity in the presence of 1.0-5.0 mM CaCl2 . Optimal concentration is 1 mM.

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Data Sheet - LIQUID
Safety Data Sheet - LIQUID

Data Sheet - LYOPHILIZED
Safety Data Sheet - LYOPHILIZED