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Heparinase III - Research Grade PN 50-012 and 50-012-001

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Heparinase III Research Grade Data Sheet


Heparin sulfate eliminase; heparitinase I


Flavobacterium heparinum (recombinant)
EC Number

CAS Number


Catalyzed Reaction

The enzyme cleaves selectively, via an elimination mechanism, sulfated polysaccharide chains containing 1-4 linkages between hexosamines and glucuronic 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 is active only towards heparan sulfate and does not cleave heparin or low molecular weight heparins.

Substrate Specificity

Heparinase III cleaves heparan sulfate exclusively, and does not cleave unfractionated heparin or low molecular weight heparins.

  • Molecular weight: 73,202 Da
  • Isoelectric point: 9.6 – 9.9
  • pH optimum for activity: 7 - 8
  • pH range for activity: 5.5 – 9
  • Optimal testing temperature range: 20 ° C – 37 ° C
  • Optimal storage temperature: –70 ° C

≥ 95 % by reversed phase HPLC analysis.

Hep III, Graph 5764

Specific Activity

>45 IU/mg

One international unit (IU) is defined as the amount of enzyme that will liberate 1.0 µmole unsaturated oligosaccharides from heparan sulfate per minute at 30 ° C and pH 7.5.

  • PN 50-012 (vial of 0.5 IU): Expiration is 30 months from manufacturing date, frozen at – 70 ° C in aqueous buffers containing Sodium Chloride, Sodium Phosphate and Sucrose 5%.
  • PN 50-012-001 (vial of 0.1 IU): Expiration is 30 months from manufacturing date, frozen at – 70 ° C in aqueous buffers containing Sodium Chloride, Sodium Phosphate and Sucrose 5%.
  • As a research reagent (glycosaminoglycan degradation).
  • For the preparation of disaccharides of heparan sulfate and the preparation of oligosaccharide libraries.

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.

  • 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.

  • “Isolation and Expression in Escherichia coli of hepB and hepC, Genes Coding for the Glycosaminoglycan-Degrading Enzymes Heparinase II and Heparinase III, Respectively, from Flavobacterium heparinum”.HongSheng Su, Françoise Blain, Roy A. Musil, Joseph J.F. Zimmermann, KangFu Gu and D. Clark Bennett, in Applied and Environmental Microbiology (1996): 2723-2734.

  • “Heparinase III from Flavobacterium heparinum: Cloning and Recombinant Expression in Escherichia coli”. R. Godavarti, M. Davis, G. Venkataraman, C. Cooney, R. Langer and R. Sasisekharan, in Biochemical and Biophysical Research Communications (1996) 225: 751-758.

  • “Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor”. I. Vlodavsky, H-Q. Miao, P. Danagher and D. Ron, in Cancer and Metastasis Reviews (1996) 15(2): 177-186.

  • “Control of Cell Proliferation by Heparan Sulfate and Heparin-Binding Growth Factors”. I. Vlodavsky, H-Q. Maio, R. Atzmon, E. Levi, J. Zimmermann, R. Bar-Shavit, T. Peretz and S. Ben-Sasson, in Thrombosis and Haemostasis (1995) 74(1): 534-540.

  • “Heparinase III Exerts Endothelial and Cardioprotective Effects in Feline Myocardial Ischemia-Reperfusion Injury”. R. Hayward, T.O. Nossuli and A.M. Lefer, in J. Pharmacology and Experimental Therapeutics (1997) 283: 1032-1038.

  • “IBT 9302 (Heparinase III): a novel enzyme for the management of reperfusion injury-related vascular damage, restenosis and wound healing”. P. Silver, in Exp. Opin. Invest. Drugs (1998) 7(6): 1003-1014.

  • “Cellular mechanisms of heparinase III protection in rat traumatic shock”.R.Hayward, R. Scalia, B. Hopper, J. Appel III and A. Lefer, in Am. J. Physiol. (1998) 275 (Heart Circ. Physiol. 44): H23-H30.

  • “Heparinase III limits rat arterial smooth muscle cell proliferation in vitro and in vivo”. P. Silver, J-P. Moreau, E. Denholm, Y.Q. Lin, L. Nguyen, C. Bennett, A. Recktenwald, D. DeBlois, S. Baker, S. Ranger in Euro. J. Pharmacol. (1998) 351:79-83.