324726
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.
Synonym(s):
Endo-β-N-acetylglucosaminidase F2, Endo F2
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About This Item
Recommended Products
recombinant
expressed in E. coli
Quality Level
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
Related Categories
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.
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
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (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)
Articles
N-Linked Glycan Strategies.
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