Description
Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides.
Abbr
Heparinase II, Recombinant (Bacteroides eggerthii)
Species
Bacteroides eggerthii
Product Overview
Bacteroides Heparinase II cloned from Bacteroides eggerthii, also called Heparin Lyase II, is a low specificity enzyme that is active on both heparin and heparan sulfate. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. Similar to Flavobacterium heparinum Heparinase II, Bacteroides Heparinase II cleaves the glycosidic bond between N-sulfated and glucuronic or iduronic acid residues. 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.
Form
100 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), 1 mM Na2EDTA and 5 mM CaCl2
Purity
> 95% determined by SDS-PAGE
Concentration
4,000 units/ml
Unit Definition
One unit is defined as the amount of enzyme that will liberate 1.0 μmol unsaturated oligosaccharides from porcine mucosal heparin per minute at 30°C and pH 7.0 in a total reaction volume of 100 μl.
Synonyms
Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III; Heparin lyase II; Heparinase II
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