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Sigma-Aldrich

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.

Synonyme(s) :

Endo-β-N-acetylglucosaminidase F1, Endo F1

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About This Item

Numéro de classification (Commission des enzymes):
3.2.1.96 (BRENDA, IUBMB)
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli

Niveau de qualité

100

Conjugué

(N-linked)

Forme

liquid

Activité spécifique

≥16 units/mg protein
≥17 units/mL

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

do not freeze

Activité étrangère

Proteases, none detected

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Catégories apparentées

Description générale

Note: 1 mU = 1 milliunit.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F1 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and hybrid, but not complex oligosaccharides. Core fucosylation reduces activity by 50 fold. Endo F1 will hydrolyze sulfate containing high mannose chains. 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.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F1 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and hybrid, but not complex oligosaccharides. Core fucosylation reduces activity by 50 fold. Endo F1 will hydrolyze sulfate containing high mannose chains. 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.

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

One unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1.0 µmol denatured ribonuclease B per min at 37°C, pH 5.5.

Forme physique

In 20 mM Tris-HCl, pH 7.5.

Autres remarques

Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.

Informations légales

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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

A L Tarentino et al.
The Journal of biological chemistry, 267(6), 3868-3872 (1992-03-06)
A full-length insert for the endo-beta-N-acetylglucosaminidase (Endo) F1 gene was located on a 2,200-base pair EcoRI fragment of genomic DNA and cloned into the plasmid vector Bluescript. Transformed Escherichia coli cells expressed Endo F1 activity very well, but the enzyme
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)
Thapakorn Jaroentomeechai et al.
Nature communications, 13(1), 6325-6325 (2022-10-25)
The ability to reconstitute natural glycosylation pathways or prototype entirely new ones from scratch is hampered by the limited availability of functional glycoenzymes, many of which are membrane proteins that fail to express in heterologous hosts. Here, we describe a

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