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Merck

324726

Endoglycosidase F2

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

Sinónimos:

Endo-β-N-acetylglucosaminidase F2, Endo F2

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Número CE:
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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Nombre del producto

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

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

Quality Level

100

storage temp.

2-8°C

Categorías relacionadas

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)

Clase de almacenamiento

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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)
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

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