Heparinase II(derived from Flavobacterium heparinum)

Bacterial heparinase II, also known as heparin lyase II, is a enzyme cloned from Flavobacterium heparinum and expressed in E. coli.

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    Bacterial heparinase II, also known as heparin lyase II, is a enzyme cloned from Flavobacterium heparinum and expressed in E. coli. Heparinase II can degrade heparin and dermatan sulfate, making it a powerful tool for heparin structure research, clinical diagnostics, and industrial quality control.

    Heparinase II cleaves heparan sulfate at the α(1→4) linkages between hexosamine and uronic acid residues (glucuronic acid and iduronic acid), and can also mediate controlled depolymerization of heparin, primarily yielding disaccharides. This reaction produces oligosaccharide products containing unsaturated uronic acids—mainly disaccharides—which can be detected by UV spectroscopy at 232 nm.

    Product Applications

    Heparinase II can be used to degrade heparin for structural analysis, such as determining the 1,6‑ring‑closure rate of enoxaparin sodium and analyzing the disaccharide profile of heparin sodium; it is also employed in combination with heparinase I and heparinase III to prepare low‑molecular‑weight heparin (LMWH); it degrades crude heparin to enable source‑identification via qPCR; and it degrades heparin and dermatan sulfate to produce heparin disaccharides and heparin oligosaccharides.

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