P0736S,  Bacteroides Heparinase II - 80 units

P0736S, Bacteroides Heparinase II - 80 units

P0737S,  Bacteroides Heparinase III - 14 units

P0737S, Bacteroides Heparinase III - 14 units

P0737L, Bacteroides Heparinase III - 35 units

4.797,49 RON

Bacteroides Heparinase III (also called Heparin Lyase III) is cloned from Bacteroides eggerthii. It is active on both heparin and heparan sulfate.

SKU
NEB_P0737L

Bacteroides Heparinase III (also called Heparin Lyase III) is cloned from Bacteroides eggerthii. It is active on both heparin and heparan sulfate.

Bacteroides Heparinase III can cleave the glycosidic bond between hexosamines and either iduronic acid or glucuronic acid residues. It is active in the presence of 6-sulfation. The reaction yields oligosaccharide products containing unsaturated uronic acids, which can be detected by UV spectroscopy at 232 nm

  • Recombinant enzyme with no detectable glycosidase, sulfatase or uronidase contaminating activities 
  • ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
  • Optimal activity and stability for up to 12 months when stored in solution at -80°C
  • Optimal for cleavage of heparan sulfate and heparin with domains of low sulfation

Product Source

Cloned from Bacteroides Eggerthii and expressed in E. coli.

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Price 4.031,50 RON (preturile sunt fara TVA)
Description

Bacteroides Heparinase III (also called Heparin Lyase III) is cloned from Bacteroides eggerthii. It is active on both heparin and heparan sulfate.

Bacteroides Heparinase III can cleave the glycosidic bond between hexosamines and either iduronic acid or glucuronic acid residues. It is active in the presence of 6-sulfation. The reaction yields oligosaccharide products containing unsaturated uronic acids, which can be detected by UV spectroscopy at 232 nm

  • Recombinant enzyme with no detectable glycosidase, sulfatase or uronidase contaminating activities 
  • ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
  • Optimal activity and stability for up to 12 months when stored in solution at -80°C
  • Optimal for cleavage of heparan sulfate and heparin with domains of low sulfation

Product Source

Cloned from Bacteroides Eggerthii and expressed in E. coli.