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Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli

Name: Endoglycosidase F2, <i>Elizabethkingia meningosepticum</i>, Recombinant, <i>E. coli</i>
Brand: MM

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.

Synonym(s):

Endo-β-N-acetylglucosaminidase F2, Endo F2

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About This Item

Enzyme Commission number:

3.2.1.96 (BRENDA, IUBMB)

UNSPSC Code:

12352202

NACRES:

NA.54

recombinant

expressed in E. coli

Quality Level

100

conjugate

(N-linked)

form

liquid

specific activity

≥20 units/mg protein
≥5 units/mL

manufacturer/tradename

Calbiochem^®

storage condition

do not freeze

foreign activity

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

shipped in

wet ice

storage temp.

2-8°C

General description

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.

Warning

Toxicity: Standard Handling (A)

Unit Definition

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.

Physical form

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

Other Notes

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.

Legal Information

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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High-level expression of the Endo-beta-N-acetylglucosaminidase F2 gene in E.coli: one step purification to homogeneity.

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

Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression.

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

Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans.

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.