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324726

Endoglycosidase F2

Name: Endoglycosidase F2
Brand: MM

Targets complex N-glycans, suitable for Mass Spectrometry, from Elizabethkingia meningosepticum, recombinant, expressed in E. coli

Synonym(s):

Endo-β-N-acetylglucosaminidase F2, Endo F2

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About This Item

EC Number:

3.2.1.96 (BRENDA, IUBMB)

UNSPSC Code:

12352202

NACRES:

NA.54

Specific activity:

≥20 units/mg protein, ≥5 units/mL

Recombinant:

expressed in E. coli

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Properties

Product Name

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.

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

Description

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.

Physical form

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

Other Notes

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.

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

Disclaimer

Toxicity: Standard Handling (A)

Storage Class

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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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.

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

Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum.