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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)

Sinonimo/i:

Heparin lyase II

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10 UNITS
315,00 €
25 UNITS
622,00 €
100 UNITS
2.070,00 €

315,00 €

Per informazioni sulla disponibilità, contatta il Servizio Clienti.
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Cambia visualizzazione
10 UNITS
315,00 €
25 UNITS
622,00 €
100 UNITS
2.070,00 €

About This Item

Numero CAS:
149371-12-0
Numero MDL:
MFCD00131319
Codice UNSPSC:
12352204
NACRES:
NA.54

315,00 €

Per informazioni sulla disponibilità, contatta il Servizio Clienti.

Origine biologica

bacterial (Flavobacterium heparinum)

Livello qualitativo

200

Coniugato

conjugate (Glucosaminoglycan)

Stato

lyophilized powder

Attività specifica

≥100 units/mg protein (enzyme + BSA)

PM

84.1 kDa

Temperatura di conservazione

−20°C

Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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.

Definizione di unità

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.

Altre note

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
0000362674
0000316874
0000344868
0000362674
0000340605

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McLean, M.W., et al.
Proc. 8th Int. Symp. Glycoconjugates, 1, 73-73 (1985)
PCR-sequence-specific primer typing of HLA class I and class II alleles.
Mike Bunce
Methods in molecular biology (Clifton, N.J.), 210, 143-171 (2002-11-05)
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
R F Sewell et al.
The Biochemical journal, 264(3), 777-783 (1989-12-15)
Xyloside-initiated 35SO4(2-)-labelled glycosaminoglycans were isolated from the medium of cultured bovine glomeruli and covalently coupled to Sepharose 4B to construct a solid-phase substrate suitable for the detection of endoglycosidases. The substrate is rendered specific for heparitinase by prior digestion with
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