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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)

Synonyme(s) :

Heparinase I and Heparinase III blend

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About This Item

Numéro de classification (Commission des enzymes):
4.2.2.7 (BRENDA, IUBMB)
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Flavobacterium heparinum)

Niveau de qualité

200

Conjugué

conjugate (Glucosaminoglycan)

Forme

lyophilized powder

Activité spécifique

≥200 units/mg protein

Concentration

≥200 unit/mg protein (enzyme + BSA)

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

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

Actions biochimiques/physiologiques

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.

Conditionnement

Sold on the basis of Heparinase I units

Définition de l'unité

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.

Autres remarques

Enzyme Commission Numbers: 4.2.2.7 Hep I and 4.2.2.8 Hep III

Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
0000312746
0000312745
0000312744
0000249053
0000249052

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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
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
Retinal proteoglycans act as cellular receptors for basement membrane assembly to control astrocyte migration and angiogenesis
Tao C and Zhang X
Cell Reports, 17(7), 1832-1844 (2016)
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)
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.
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