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H6512

Sigma-Aldrich

Heparinase II from Flavobacterium heparinum

Lyophilized powder stabilized with approx. 25% bovine serum albumin, lyophilized powder, ≥100 units/mg protein (enzyme + BSA)

Synonyme(s) :

Heparin lyase II

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About This Item

Numéro CAS:
149371-12-0
Numéro MDL:
MFCD00131319
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Flavobacterium heparinum)

Niveau de qualité

200

Conjugué

conjugate (Glucosaminoglycan)

Forme

lyophilized powder

Activité spécifique

≥100 units/mg protein (enzyme + BSA)

Poids mol.

84.1 kDa

Température de stockage

−20°C

Description générale

Heparinase II is one of three key heparin-degrading enzymes of Flavobacterium heparinum (also known as Pedobacter heparinus1). It belongs to the polysaccharide lyases family PL21.

Application

Heparinase II from Flavobacterium heparinum has been used:
  • for digestion of heparin sulfate during exosome isolation
  • for digestion of heparin sulfate in notochordal cell conditioned media (NCCM) to investigate the content of glycosaminoglycans in NCCM
  • as a component of digestion buffer during cell surface glycan processing
  • as a component of heparin lyase (HSase) mix to remove the heparin sulfate on the 293ͰT/ACE2 cell surface and study the effect of histones on the infectivity of pseudovirus

Actions biochimiques/physiologiques

Heparinase II cleaves heparan sulfate, and to a lesser extent heparin (relative activity about 2:1), at the α (1-4) linkages between hexosamines and uronic acid residues (both glucuronic and iduronic), yielding mainly disaccharides. Heparinase II has the broadest substrate specificity of the three heparinases Heparinase enzymes helps in decoding the complex structures of substrates. Heparin interferes with DNA transcription in PCR and in reverse transcription of RNA. Heparinase II has been used to remove heparin for downstream analysis of genomic DNA.

Définition de l'unité

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.0 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units.

Autres remarques

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Devina Purmessur et al.
The spine journal : official journal of the North American Spine Society, 15(5), 1060-1069 (2015-02-11)
Painful human intervertebral discs (IVDs) exhibit nerve growth deep into the IVD. Current treatments for discogenic back pain do not address the underlying mechanisms propagating pain and are often highly invasive or only offer temporary symptom relief. The notochord produces
Moffat, C.F., et al.
Proc. 8th Int. Symp. Glycoconjugates, 1, 79-79 (1985)
McLean, M.W., et al.
Proc. 8th Int. Symp. Glycoconjugates, 1, 73-73 (1985)
David Shaya et al.
The Journal of biological chemistry, 285(26), 20051-20061 (2010-04-21)
Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Recently, we determined the crystal structure of HepII from Pedobacter heparinus (previously known as Flavobacterium heparinum) in complex with a
Tianji Ma et al.
Biosensors & bioelectronics, 137, 207-212 (2019-05-18)
The heparin contamination by oversulfated chondroitin (OSCS) was at the origin of one major sanitary problem of last decade. Here we propose a novel strategy to detect OSCS from heparin solution based on conical nanopore functionalized with poly-L-lysine deposition to
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