Bacteroides Heparinase II (also called Heparin Lyase II) is cloned from Bacteroides eggerthii. It is a low specificity enzyme that is active on both heparin and heparan sulfate.
Bacteroides Heparinase II cleaves the glycosidic bond between N-sulfated and glucuronic or iduronic acid residues. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm.
When used alone this enzyme rarely yields complete depolymerization of a polysaccharide chain, however disaccharide analysis is enhanced when used in combination with Heparinase I and III.
• Recombinant enzyme with no detectable glycosidase, sulfatase or uronidase contaminating activities
• ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
• Optimal activity and stability for up to 12 months when stored in solution at -80°C
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