Heparinase I, from Flavobacterium Heparinum CAS NO.9025-39-2

Heparinase I cleaves selectively, via and 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 antithroombin III binding pentasaccharide domain in the heparin molecule. 

Properties

Molecular weight: 42.8 kDa |

Isoelectric point: 9.3 – 9.5

pH optimum for activity: 7.4

pH range for activity: 4 – 9

Optimal temperature range: 20 ℃ – 37 ℃

Purity: ≥ 98 % by reversed phase HPLC analysis

Protein impurities: < 0.1%

Specific Activity: > 400 IU/mg (max. 417 IU/mg)

Concentration: 10 IU/mL

Standard: 0.1 IU, 1.0 IU, or customized standard

Unit Definition: One international unit (IU) of heparinase I is defined as the amount of enzyme that will liberate 1.0 μmole unsaturated oligosaccharides from porcine mucosal heparin per minute at 35 ℃ and pH 7.0.

Stability: Expiration of heparinase I is 12 months from manufacturing date, frozen at -20 ℃ in PBS.