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H3917

Sigma-Aldrich

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

Enzyme Commission number:
4.2.2.7 (BRENDA, IUBMB)
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Flavobacterium heparinum)

Quality Level

200

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.

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Farizeh Aalam et al.
PLoS pathogens, 16(10), e1008968-e1008968 (2020-10-20)
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
R Sasisekharan et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(4), 1524-1528 (1994-02-15)
Neovascularization is associated with the regulation of tissue development, wound healing, and tumor metastasis. A number of studies have focused on the role of heparin-like molecules in neovascularization; however, little is known about the role of heparin-degrading enzymes in neovascularization.
IL-2 inducible kinase ITK is critical for HIV-1 infection of Jurkat T-cells
Hain A, et al.
Scientific reports, 8(1), 3217-3217 (2018)
Glycosaminoglycans contribute to extracellular matrix fiber recruitment and arterial wall mechanics
Mattson JM, et al.
Biomechanics and Modeling in Mechanobiology, 16(1), 213-225 (2017)
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
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