Flavobacterium Heparinases II

Heparinase II, also known as Heparin Lyase II or Heparitinase II is catalytically active on both heparin and sulfated domains of heparan sulfate in an endolytic manner. It cleaves less selectively, via an elimination mechanism, sulfated polysaccharide chains containing 1-4 linkages between hexosamines and uronic acid residues (both iduronic and glucuronic acid residues) on the nonreducing end. The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. Complete depolymerization of polysaccharide chains is improved when Heparinase II is used in combination with Heparinase I and III for the disaccharide analysis.

The enzyme cleaves both heparin and heparan sulfate, with the heparan sulfate activity being 2-fold higher than the heparin activity.

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

  • Heparinase II is O-glycosylated at Thr-134
  • Purity: ≥ 90 % by reversed phase HPLC analysis
  • IBEX liquid heparinase II has optimal activity and stability for up to 2.5 years when stored frozen at -70°C
  • IBEX lyophilized heparinase II has optimal activity and stability for up to two years when stored at 2-8oC
  • Calcium is inhibitory

To request a quote, click the button below:

Data Sheet - LIQUID
Safety Data Sheets - LIQUID

Safety Data Sheet - Lyophilized