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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)

Sinónimos:

Heparinase I and Heparinase III blend

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About This Item

Comisión internacional de enzimas:
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

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «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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