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Heparinase I - Diagnostic Grade Datasheet
Synonyms	Heparinase; heparin lyase; heparin eliminase
Source	Flavobacterium heparinum (recombinant)
EC Number CAS_Number	4.2.2.7 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 Specificity	Heparin; heparan sulfate (specific activity with heparin is approx. 3 times higher than with heparan sulfate).
Properties:	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 temperature range: 20 ° C – 37 ° C
Purity	≥ 95 % by reversed phase HPLC analysis.
Specific Activity	>90-110 IU/mg 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 ° C and pH 7.0. (One Unit (U) is also defined in other preparations as 1 U forms 0.1 µmol of unsaturated uronic acid per hour at 25° C and pH 7.5; 1 IU is equivalent to 600U).
Stability	Expiration is primarily established at 3 years after manufacturing. The Heparinase I is kept frozen at -70 ° C in aqueous buffers containing Sodium Phoshate or Sucrose 5%

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