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324726

Sigma-Aldrich

Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli

Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli cleaves asparagine-linked or free oligomannose and biantennary complex oligosaccharides. It is not active above pH 6.0.

Sinonimo/i:

Endo-β-N-acetylglucosaminidase F2, Endo F2

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About This Item

Classificazione EC (Enzyme Commission):
Codice UNSPSC:
12352202
NACRES:
NA.54

Ricombinante

expressed in E. coli

Livello qualitativo

Coniugato

(N-linked)

Forma fisica

liquid

Attività specifica

≥20 units/mg protein
≥5 units/mL

Produttore/marchio commerciale

Calbiochem®

Condizioni di stoccaggio

do not freeze

Attività estranea

N-acetylglucosaminidase, α- and β-galactosidase, α-mannosidase, neuraminidases, proteases, none detected

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

Descrizione generale

Note: 1 mU = 1 milliunit.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F2 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and biantennary complex oligosaccharides from glycoproteins. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore is more suitable for deglycosylation of native proteins. This enzyme is not active above pH 6.0.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F2 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and biantennary complex oligosaccharides from glycoproteins. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore, is more suitable for deglycosylation of native proteins.

Attenzione

Toxicity: Standard Handling (A)

Definizione di unità

One unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1 µmol porcine fibrinogen per min at 37°C, pH 4.5.

Stato fisico

In 25 mM NaCl, 10 mM sodium acetate buffer, pH 4.5.

Altre note

Reddy, A., et al. 1998. Glycobiology 8, 633.
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1993. J. Biol. Chem. 268, 9702.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.

Note legali

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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A Reddy et al.
Glycobiology, 8(6), 633-636 (1998-06-11)
The Endo F2gene was overexpressed in E.coli as a fusion protein joined to the maltose-binding protein. MBP-Endo F2was found in a highly enriched state as insoluble, inactive inclusion bodies. Extraction of the inclusion bodies with 20% acetic acid followed by
A L Tarentino et al.
The Journal of biological chemistry, 268(13), 9702-9708 (1993-05-05)
The genes for Flavobacterium meningosepticum Endo (endoglycosidase) F2 and Endo F3 were cloned, and their nucleotide sequences were determined. The deduced amino acid sequences were verified independently to a large extent by direct peptide microsequencing of 66 and 84% of
R B Trimble et al.
The Journal of biological chemistry, 266(3), 1646-1651 (1991-01-25)
Flavobacterium meningosepticum endo-beta-acetyl-glucosaminidase F preparations have been resolved by hydrophobic interaction chromatography on TSK-butyl resin into at least three activities designated endo F1, endo F2 and endo F3 each with a unique substrate specificity. The 32-kDa endo F1 protein is
Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum.
A L Tarentino et al.
Methods in enzymology, 230, 44-57 (1994-01-01)

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