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324727

Sigma-Aldrich

Endoglycosidase F3

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

Synonym(s):

Endo-β-N-acetylglucosaminidase F3, Endo F3

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200 MI.U.
$577.00

$577.00

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About This Item

EC Number:
3.2.1.96 (BRENDA, IUBMB)
UNSPSC Code:
12352202
NACRES:
NA.54

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Product Name

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.

recombinant

expressed in E. coli

Quality Level

100

conjugate

(N-linked)

form

liquid

specific activity

≥30 units/mg protein
≥5 units/mL

manufacturer/tradename

Calbiochem®

storage condition

do not freeze

foreign activity

Proteases, none detected

shipped in

wet ice

storage temp.

2-8°C

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This Item
324725324726E2264
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.

Sigma-Aldrich

324727

Endoglycosidase F3, Elizabethkingia meningosepticum, Recombinant, E. coli

Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli cleaves asparagine-linked or free oligomannose and hybrid. Suitable for deglycosylation of native proteins.

Sigma-Aldrich

324725

Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli

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.

Sigma-Aldrich

324726

Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli

Endoglycosidase F3 from Elizabethkingia miricola recombinant, expressed in E. coli, 30 U/mg

Sigma-Aldrich

E2264

Endoglycosidase F3 from Elizabethkingia miricola

specific activity

≥30 units/mg protein, ≥5 units/mL

specific activity

≥16 units/mg protein, ≥17 units/mL

specific activity

≥20 units/mg protein, ≥5 units/mL

specific activity

30 U/mg

form

liquid

form

liquid

form

liquid

form

solution

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

storage condition

do not freeze

storage condition

do not freeze

storage condition

do not freeze

storage condition

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

General description

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.

Other Notes

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.
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.

Legal Information

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

Disclaimer

Toxicity: Standard Handling (A)

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (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
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)
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

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