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E0639

Sigma-Aldrich

Endoglycosidase F2 from Elizabethkingia miricola

recombinant, expressed in E. coli, 20 U/mg

Synonyme(s) :

Endoglycosidase F2, Endoglycosidase F2 from Elizabethkingia meningoseptica

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About This Item

Numéro CAS:
37278-88-9
Numéro de classification (Commission des enzymes):
3.2.1.96 (BRENDA, IUBMB)
Numéro MDL:
MFCD00151069
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

200

Conjugué

(N-linked)

Forme

solution

Activité spécifique

20 U/mg

Poids mol.

32 kDa

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Conditionnement

Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5

Définition de l'unité

One unit will release N-linked oligosaccharides from 1 μmole of denatured porcine fibrinogen in 1 minute at 37 °C, pH 4.5.

Forme physique

Aseptically filled solution in 10 mM sodium acetate, 25 mM sodium chloride, pH 4.5

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificats d'analyse (COA)

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PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE), for proteomics

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

Valentina Botti et al.
PloS one, 6(8), e23838-e23838 (2011-08-23)
Hepatitis C Virus E1E2 heterodimers are components of the viral spike. Although there is a general agreement on the necessity of the co-expression of both E1 and E2 on a single coding unit for their productive folding and assembly, in
M V Padkina et al.
Prikladnaia biokhimiia i mikrobiologiia, 46(4), 448-455 (2010-09-29)
The HuIFNA16, HuIFNB, and BoIFNG genes encoding human [alpha]16, beta-interferons and bovine gamma-interferon were cloned under the control of the yeast Pichia pastoris AOX1 gene promoter. The yeast strains producing heterologous interferons intracellularly and extracellularly were constructed. There was no
Roger S Zou et al.
Aging, 3(10), 968-984 (2011-10-13)
A distinct conformational transition from the α-helix-rich cellular prion protein (PrPC) into its β-sheet-rich pathological isoform (PrPSc) is the hallmark of prion diseases, a group of fatal transmissible encephalopathies that includes spontaneous and acquired forms. Recently, a PrPSc-like intermediate form
Yusuke Tomabechi et al.
Carbohydrate research, 345(17), 2458-2463 (2010-10-12)
To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-β-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to
Isabelle Chantret et al.
PloS one, 5(7), e11734-e11734 (2010-07-30)
During mammalian protein N-glycosylation, 20% of all dolichol-linked oligosaccharides (LLO) appear as free oligosaccharides (fOS) bearing the di-N-acetylchitobiose (fOSGN2), or a single N-acetylglucosamine (fOSGN), moiety at their reducing termini. After sequential trimming by cytosolic endo beta-N-acetylglucosaminidase (ENGase) and Man2c1 mannosidase
Afficher tous les articles scientifiques apparentés

Articles

Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

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