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Heparinase enzymes


Heparinase enzymes (heparin lyase enzymes) extracted from natural strains of Flavobacterium heparinum.  Our heparinases are natural not recombinant enzymes, folding under normal cell conditions resulting in highly active products.

The specialist method of preparation gives baseline separation between the three heparinases producing very pure individual enzyme species.

In order to preserve high activity, the enzymes are supplied as frozen solutions and delivered world wide by international courier.

The enzymes are stabilized with 0.1-0.2% BSA (Sigma A4378), 0.22um-sterile filtered and dispensed into sterile vials.


The enzymatic degradation of heparin and/or heparan sulphate.

Suitable for USP Chemical Tests / ⟨207⟩ 1,6-Anhydro Derivative for Enoxaparin Sodium.

International Units

The package size for the Heparinase enzymes is defined in International Units (IU) – one international unit is “the amount of enzyme that will liberate 1.0 μmole of product per minute from a heparin or heparan sulphate substrate at 30º C” (Product is unsaturated saccharides)

Please email [email protected] for any questions, for a quote or to place and order

Heparinase I (Hep I) EC

Degrades heparin and the S-domains of heparan sulfate.

Catalyses the eliminative scission of the glycosidic linkage between N-sulfated glucosamine (GlcNSO3) and 2-O-sulfated iduronic acid (IdoA,2SO3). The IdoA,2SO3 residue is essential for the activity of Heparinase I while 6-O-sulfation of GlcNSO3 enhances enzyme activity.

Technical Notes

The disaccharide cleaved by Heparinase I is common in heparin but it is quite rare in HS where it is confined to the sulfated domains. Thus Heparinase I will attack HS only in the S-domains bringing about limited scission of the polymer chain. This is a very valuable and under exploited property of Heparinase I. For example Heparinase I can be used to determine the spacing between S-domains in HS. This spacing is reflected in the size of the HS fragments that resist the action of the enzyme. Heparinase I can also be used to identify biological properties of HS that depend upon the integrity of the S-domains. For example HS-activation of fibroblast growth factor 2 (FGF2) is inhibited by treatment with Heparinase I (but not by Heparinase III).

Heparinase II (Hep II) EC number not assigned

Degrades heparin and heparan sulfate

Catalyses the eliminative scission of the glycosidic linkages between N-sulfated or N-acetylated glucosamine and glucuronic or iduronic acid. This is a broad activity enzyme that tolerates O-sulfation of the uronic acid and glucosamine residues.

Technical notes

This low specificity enzyme attacks most linkages in heparin and HS but it does not effect complete depolymerisation of either GAG. It is very useful for analysis of disaccharide composition but its effectiveness is enhanced when used in combination with Heparinase I and Heparinase III. Heparinase II will cleave heparin and HS at N-unsubstituted glucosamine (GlcNH3+) residues; in contrast the GlcNH3+-GlcA (or IdoA) linkage is resistant to Heparinase I and Heparinase III.

Heparinase III (Hep III/Heparitinase) EC

Degrades heparan sulfate (HS)
Catalyses the eliminative scission of glycosidic linkages between N-sulfated or N-acetylated glucosamine (GlcNSO3 or GlcNAc) and glucuronic acid (GlcA)

Technical notes

Heparinase III (Heparitinase) acts on Heparan Sulphate in regions of low sulfation and it has little activity against heparin. The preferred substrates for heparinase III are N-Acetylated or N-sulfated glucosamines linked to glucuronic acid. (i.e. GlcNAc/ GlcNSO3 1 – 4 GlcA). In consequence it acts primarily in the non-sulfated domains (NAc domains) and transition zones of HS whereas the highly sulfated S-domains are resistant to Heparinase III. The enzyme tolerates C-6 sulfation of amino sugars. Heparinase III has weak activity with disaccharides containing Iduronic Acid (IdoA) and its action is blocked if the iduronate residue is sulfated at C-2 (IdoA, 2SO3).

The Heparinase III resistant S-domains in HS have a heparin-like structure being mainly composed of GlcNSO3 1 – 4 IdoA,2SO3 repeat units with variable O-sulfation at C-6 of the GlcNSO3 residue. They vary in length form 3 to 9 disaccharide units. The patterns and densities of 6-O-sulfate groups along S-domains are an important determinant of their protein binding specificities.

The selectivity of Heparinase III can be exploited for the preparation of S-domains from HS. High resolution gel filtration will separate the different size classes of S-domain and these can be further subfractionated by SAX-HPLC according to sulfate content and patterning.

Product Catalog No Qty £
  1. Heparinase I
    Heparinase I - 0.1 IU HEP-ENZ I 0.1 IU 154.00 Enquire Now
    Heparinase I - 0.5 IU HEP-ENZ I 0.5IU 0.5 IU 440.00 Enquire Now
    Heparinase I - 2.0 IU HEP-ENZ I 2.0IU 2.0 IU 850.00 Enquire Now
    Heparinase I - 5.0 IU HEP-ENZ I 5.0IU 5.0 IU 1900.00 Enquire Now
  2. Heparinase II
    Heparinase II - 0.1 IU HEP-ENZ II 0.1 IU 484.00 Enquire Now
    Heparinase II - 0.5 IU HEP-ENZ II 0.5IU 0.5 IU 2200.00 Enquire Now
    Heparinase II - 1.0 IU HEP-ENZ II 1.0IU 1.0 IU 3993.00 Enquire Now
  3. Heparinase III
    Heparinase III - 0.1 IU HEP-ENZ III 0.1 IU 319.00 Enquire Now
    Heparinase III - 0.5 IU HEP-ENZ III 0.5IU 0.5 IU 880.00 Enquire Now
    Heparinase III 1.0 IU HEP-ENZ III 1.0IU 1.0 IU 1540.00 Enquire Now
    Heparinase III - 2.0 IU HEP-ENZ III 2.0IU 2 IU 2750.00 Enquire Now

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