324727
Endoglycosidase F3, Elizabethkingia meningosepticum, Recombinant, E. coli
Endoglycosidase F3, Elizabethkingia meningosepticum, Recombinant, E. coli, cleaves asparagine-linked or free biantennary and triantennary complex, and Man3GlcNAc oligosaccharides from glycoproteins.
Synonym(e):
Endo-β-N-acetylglucosaminidase F3, Endo F3
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About This Item
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Konjugat
(N-linked)
Form
liquid
Spezifische Aktivität
≥30 units/mg protein
≥5 units/mL
Hersteller/Markenname
Calbiochem®
Lagerbedingungen
do not freeze
Fremdaktivität
Proteases, none detected
Versandbedingung
wet ice
Lagertemp.
2-8°C
Allgemeine Beschreibung
Recombinant, Elizabethkingia meningosepticum endoglycosidase F3 expressed in E. coli. Cleaves asparagine-linked or free biantennary and triantennary complex, and Man3GlcNAc oligosaccharides from glycoproteins. This enzyme 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 residue. Core fucosylation increases the activity of Endo F3 up to 40 fold. Exhibits no activity on high mannose and hybrid molecules. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore is more suitable for deglycosylation of native proteins.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F3 expressed in E. coli. Cleaves asparagine-linked or free biantennary and triantennary complex, and Man3GlcNAc oligosaccharides from glycoproteins. This enzyme 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 residue. Core fucosylation increases the activity of Endo F3 up to 40 fold. Exhibits no activity on high mannose and hybrid molecules. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore is more suitable for deglycosylation of native proteins.
Warnhinweis
Toxicity: Standard Handling (A)
Einheitendefinition
One unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1.0 µmol porcine fibrinogen per min at 37°C, pH 5.5.
Sonstige Hinweise
Tarentino, A.L., et al. 1995. Glycobiology 5, 599.
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.
Rechtliche Hinweise
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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A L Tarentino et al.
Glycobiology, 5(6), 599-601 (1995-09-01)
The gene for endo-beta-N-acetylglucosaminidase F3 was cloned into the high-expression vector pMAL c-2, and expressed in Escherichia coli as a fusion protein. A key step in the purification employed Poros II (HS) chromatography, which greatly facilitated isolation of the enzyme
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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