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Heparinase I（derived from Flavobacterium heparinum）

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

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Product Information
Bacterial heparinase I, also known as heparin lyase I, is a enzyme cloned from Flavobacterium heparinum and expressed in E. coli. It exhibits activity toward both the highly sulfated domains of heparin and dermatan sulfate. This reaction yields oligosaccharide products containing unsaturated uronic acids, which can be detected by UV spectroscopy at 232 nm.
Bacterial heparinase I cleaves the glycosidic bonds between N-sulfated glucosamine residues and 2-O-sulfated iduronic acid residues, as well as between 2-O-sulfated glucuronic acid residues. The 2-O-sulfation of uronic acid residues is essential for the activity of bacterial heparinase I, whereas 6-O-sulfation of GlcNS does not inhibit enzymatic activity.
Product Applications
Heparinase I can be used to study the mechanisms of heparin synthesis, degradation, and metabolism. In vitro, it can be employed to degrade heparin, thereby facilitating a deeper understanding of its biological activities. Heparinase I is also applicable for the preparation of low-molecular-weight heparins (LMWHs).

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Phone:0575-82161872

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