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Merck

H8891

Heparinase III from Flavobacterium heparinum

Lyophilized powder stabilized with approx. 25% (w/w) bovine serum albumin, ≥30 units/mg protein (enzyme + BSA)

Synonyme(s) :

Heparin Lyase III, Heparitinase I, Heparitinase from Flavobacterium heparinum

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Numéro CE :
MDL number:
Specific activity:
≥30 units/mg protein (enzyme + BSA)
Biological source:
bacterial (Flavobacterium heparinum)
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biological source

bacterial (Flavobacterium heparinum)

Quality Level

conjugate

conjugate (Glucosaminoglycan)

form

lyophilized powder

specific activity

≥30 units/mg protein (enzyme + BSA)

mol wt

70.8 kDa

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Application

Heparinase III from Flavobacterium heparinum has been used to cleave specific GAGs. It has been used to study its effect on the electrophoretic mobility of the protein reacting with the anti-aFGF (acidic fibroblast growth factor) antibody.

Biochem/physiol Actions

Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate.
Heparinase III prevents the formation of new blood vessels in vivo. It specifically degrades heparin sulphate at the HNY-I and HNY,6X-G2 links. Unlike other heparinise, heparinase III does not contain the amino acid cysteine. It contains 13 histidine residues, which is responsible for its catalytic action. This enzyme is not active towards heparin or low molecular weight heparins.

Other Notes

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

FGF binding by extracellular matrix components of Wharton's jelly
Malkowski A, et al.
Acta Biochimica Polonica, 54(2), 357-357 (2007)
Fluid shear stress primes mouse embryonic stem cells for differentiation in a self-renewing environment via heparan sulfate proteoglycans transduction
Toh YC and Voldman J
Faseb Journal, 25(4), 1208-1217 (2011)
Erin M Smith et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(51), 21683-21688 (2009-12-08)
Platelet-derived growth factor (PDGF) signaling is essential for processes involving cell motility and differentiation during embryonic development in a wide variety of organisms including the mouse, frog, zebrafish, and sea urchin. In early Xenopus laevis embryos, PDGF-AA provides guidance cues
Andrea Garolla et al.
Human reproduction (Oxford, England), 27(4), 967-973 (2012-02-09)
Human papillomavirus (HPV) infection has been demonstrated in the sperm of a large percentage of sexually active males and is associated with an impairment of sperm parameters, with a particular negative impact on sperm motility, suggesting a possible role in
A Constantinescu et al.
Thrombosis and haemostasis, 105(5), 790-801 (2010-12-22)
A thick endothelial glycocalyx contributes to the barrier function of vascular endothelium in macro- and microcirculation. We hypothesised in the current study that diet-induced hyperlipidaemia perturbs the glycocalyx, resulting in decreased dimensions of this layer and increased transendothelial lipoprotein leakage

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