324725
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.
Sinônimo(s):
Endo-β-N-acetylglucosaminidase F1, Endo F1
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About This Item
Produtos recomendados
recombinante
expressed in E. coli
Nível de qualidade
conjugado
(N-linked)
forma
liquid
atividade específica
≥16 units/mg protein
≥17 units/mL
fabricante/nome comercial
Calbiochem®
condição de armazenamento
do not freeze
atividade externa
Proteases, none detected
Condições de expedição
wet ice
temperatura de armazenamento
2-8°C
Descrição geral
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.
Advertência
Toxicity: Standard Handling (A)
Definição da unidade
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.
forma física
In 20 mM Tris-HCl, pH 7.5.
Outras notas
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.
Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
Informações legais
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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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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