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
biological source
bacterial (Flavobacterium heparinum)
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
Quality Level
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
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.
Packaging
Sold on the basis of Heparinase I units
Other Notes
Enzyme Commission Numbers: 4.2.2.7 Hep I and 4.2.2.8 Hep III
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.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
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 M Galliher et al.
Applied and environmental microbiology, 41(2), 360-365 (1981-02-01)
Heparinase production by Flavobacterium heparinum in complex protein digest medium, with heparin employed as the inducer, has been studied and improved. The maximum productivity of heparinase has been increased 156-fold over that achieved by previously published methods to 375 U/liter
Mi Gyeom Kim et al.
Scientific reports, 11(1), 3378-3378 (2021-02-11)
Cell surface heparan sulfate proteoglycan (HSPG)-mediated endocytosis results in poor yields of recombinant human bone morphogenetic proteins (rhBMPs) from CHO cell cultures. Upon incubation of rhBMP-2 and rhBMP-7 with CHO cells at 37 °C, both rhBMP-2 and rhBMP-7 bound to the
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)
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