Heparinase I Lyophilized

Heparinase I Lyophilized Powder

Heparinase I Lyophilized Powder – Research Grade PN 60-010, 60-012, 60-014

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	Heparinase I Freeze Dried Powder – Research Grade PN 60-010, 60-012, 60-014
Synonyms	Heparinase; heparin lyase; heparin eliminase
Source	Flavobacterium heparinum (recombinant)
EC Number	4.2.2.7
CAS Number	9025-39-2
Catalyzed Reaction	The enzyme cleaves selectively, via an elimination mechanism, highly sulfated polysaccharide chains containing 1-4 linkages between hexosamines and O-sulfated iduronic acid residues. The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. The enzyme also cleaves the antithrombin III binding pentasaccharide domain in the heparin molecule.
Substrate Specifity	Heparin; heparan sulfate (specific activity with heparin is approx. 3 times higher than with heparan sulfate).
Properties	Freeze-dried powder
	Molecular weight: 42,508 Da
	Isoelectric point: 9.3 – 9.5
	pH optimum for activity: 6.5 – 7.5
	pH range for activity: 4 – 9
	Optimal testing temperature range: 20 ºC – 37 ºC
	Optimal storage temperature: 5 ºC +/- 3
Purity	Made from Heparinase I (PN 50-009)≥95 % by reversed phase HPLC analysis.
Specific Activity	Approximately 100 IU/mg of proteins using the following Unit definition.
	One international unit (IU) is defined as the amount of enzyme that will liberate 1.0 µmole unsaturated oligosaccharides from porcine mucosal heparin per minute at 30 ºC and pH 7.0.
Reconstitution	Add 250 µL of water to reconstitute to its original formulation
Stability	Expiration is 24 months from manufacturing date when stored at 5ºC +/- 3.
Applications	For the in-vitro neutralization of heparin and low molecular weight heparin in blood and plasma samples before analysis.
	For the preparation of low molecular weight heparins from unfractionated heparin.
	As a research reagent (glycosaminoglycan degradation).
	For the preparation of disaccharides of heparin and the preparation of oligosaccharide libraries.
Availability	A proprietary expression system for F. heparinum and the fermentation and isolation processes developed by IBEX Pharmaceuticals allow the production of large quantities of high purity product.
References	Review: “Enzymatic Degradation of Glycosaminoglycans”. S. Ernst et al. in Critical Reviews in Biochemistry and Molecular Biology (1995), 30(5): 387-444.
	“Purification and Characterization of Heparin Lyases from Flavobacterium heparinum”. D.L. Lohse and R.J. Linhardt in J. Biol. Chem. (1992) 267: 24347-24355.
	“Purification and Characterization of Heparinase from Flavobacterium heparinum”. V.C.Yang, R.J. Linhardt, H. Bernstein, C.L. Cooney and R. Langer in J. Biol. Chem. (1985) 260(3): 1849-1857.
	“Substrate Specificity of the Heparin Lyases from Flavobacterium heparinum”. U.R.Desai, H.Wang and R.J. Linhardt in Archives of Biochemistry and Biophysics (1993) 306(2): 461-468.
	“Heparinase I from Flavobacterium heparinum. Mapping and Characterization of the Heparin Binding Domain”. R. Sasisekharan, G. Venkataraman, R. Godavarti, S. Ernst, C.L. Cooney and R. Langer in J. Biol. Chem. (1996) 271 (6): 3124-3131.
	“Cloning and Expression of Heparinase I Gene from Flavobacterium heparinum”. R. Sasisekharan, M. Bulmer, K.W. Moremen, C.L. Cooney and R. Langer in Proc. Natl. Acad. Sci. USA (1993) 90: 3660-3664.
	“Neutralase (Heparinase I) as a Potential Heparin Reversal Agent in Coronary Artery Bypass Surgery”. P.J. Silver in Management of Bleeding in Cardiovascular Surgery, edited by R. Pifarré, MD, (2000) Hanley & Belfus, Inc., Philadelphia, PA.
	“The effects of heparinase I and protamine on platelet reactivity”. T. Ammar and C.F. Fisher in Anesthesiology (1997) 86: 1382-1386.
	“Heparinase I (Neutralase) Reversal of Systemic Anticoagulation”. L.G. Michelsen, M. Kikura, J.H. Levy et al. in Anesthesiology (1996) 85: 339-346.
	“Neutralase Reverses the Anti-coagulant but not the Anti-thrombotic Activity of Heparin in a Rabbit Model of Venous Thrombosis”. P.J. Silver, R. Broughton, J. Bouthillier et al. in Thromb. Res. (1998) 91: 143-150.