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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)

Sinónimos:

Heparin lyase II

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About This Item

Número de CAS:
149371-12-0
MDL number:
MFCD00131319
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Flavobacterium heparinum)

Quality Level

200

conjugate

conjugate (Glucosaminoglycan)

form

lyophilized powder

specific activity

≥100 units/mg protein (enzyme + BSA)

mol wt

84.1 kDa

storage temp.

−20°C

General description

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

Biochem/physiol Actions

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.

Unit Definition

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.

Other Notes

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
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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