H3917
Heparinase I and III Blend from Flavobacterium heparinum
lyophilized powder, stabilized with ∼ 25% (w/w) bovine serum albumin, ≥200 unit/mg protein (enzyme + BSA)
Synonym(s):
Heparinase I and Heparinase III blend
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About This Item
Recommended Products
biological source
bacterial (Flavobacterium heparinum)
Quality Level
conjugate
conjugate (Glucosaminoglycan)
form
lyophilized powder
specific activity
≥200 units/mg protein
concentration
≥200 unit/mg protein (enzyme + BSA)
shipped in
dry ice
storage temp.
−20°C
General description
Heparinase is an inducible, non-extracellular heparin-degrading enzyme. Three types of heparinises are produced by Flavobacterium heparinum and contains specific sequences of heparin.
Application
Heparinase I and III Blend from Flavobacterium heparinum has been used in:
- the digestion of heparan sulfate from ovine vitreous
- human embryonic kidney cells
- glycosaminoglycans from arterial tissues
- P0 retinae digestion
Biochem/physiol Actions
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.
Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate.
Packaging
Sold on the basis of Heparinase I units
Unit Definition
One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using Heparin, Sodium as substrate for heparinase I.
One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using bovine kidney Heparan, Sulfate as substrate for heparinase III.
One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units. Package sizes are sold in Sigma units.
One unit will form 0.1 micromole of unsaturated uronic acid per hour at 7.5 at 25 degrees C using bovine kidney Heparan, Sulfate as substrate for heparinase III.
One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units. Package sizes are sold in Sigma units.
Other Notes
Enzyme Commission Numbers: 4.2.2.7 Hep I and 4.2.2.8 Hep III
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
含少量动物源组分生物产品
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Farizeh Aalam et al.
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Despite 25 years of research, the basic virology of Kaposi Sarcoma Herpesviruses (KSHV) in B lymphocytes remains poorly understood. This study seeks to fill critical gaps in our understanding by characterizing the B lymphocyte lineage-specific tropism of KSHV. Here, we
S Ernst et al.
Critical reviews in biochemistry and molecular biology, 30(5), 387-444 (1995-01-01)
Glycosaminoglycans (GAGs) play an intricate role in the extracellular matrix (ECM), not only as soluble components and polyelectrolytes, but also by specific interactions with growth factors and other transient components of the ECM. Modifications of GAG chains, such as isomerization
P Bashkin et al.
Journal of cellular physiology, 151(1), 126-137 (1992-04-01)
Heparan sulfate proteoglycans (HSPG) are ubiquitous constituents of mammalian cell surfaces and most extracellular matrices. A portion of the cell surface HSPG is anchored via a covalently linked glycosyl-phosphatidylinositol (Pl) residue, which can be released by treatment with a glycosyl-Pl
D A Chappell et al.
The Journal of biological chemistry, 268(19), 14168-14175 (1993-07-05)
Bovine milk lipoprotein lipase (LPL) induced binding, uptake, and degradation of 125I-labeled normal human triglyceride-rich lipoproteins by cultured mutant fibroblasts lacking LDL receptors. The induction was dose-dependent and occurred whether LPL and 125I-lipoproteins were added to incubation media simultaneously or
U R Desai et al.
Archives of biochemistry and biophysics, 306(2), 461-468 (1993-11-01)
A detailed knowledge about the substrate specificities of the heparin lyases is necessary when using these enzymes as tools for elucidating the sequence of heparin and heparan sulfate. The substrate specificity of heparin lyases I, II, and III have been
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