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Merck
CN

E2264

Sigma-Aldrich

Endoglycosidase F3 from Elizabethkingia miricola

recombinant, expressed in E. coli, 30 U/mg

Synonym(s):

Elizabethkingia miricola, Endo-β-N-acetylglucosaminidase F3, Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum

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About This Item

EC Number:
3.2.1.96 (BRENDA, IUBMB)
MDL number:
MFCD00146843
UNSPSC Code:
12352204
NACRES:
NA.32

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recombinant

expressed in E. coli

Quality Level

200

conjugate

(N-linked)

form

solution

specific activity

30 U/mg

mol wt

32 kDa

shipped in

wet ice

storage temp.

2-8°C

Related Categories

Application

Endoglycosidase F3 from Elizabethkingia miricola has been used to analyze core fucosylation and tryptic digests of serum proteins.

Biochem/physiol Actions

Cleaves asparagine-linked biantennary and triantennary complex, oligosaccharides depending on the state of core fucosylation and peptide linkage.
Endoglycosidase F3 belongs to the glycoside hydrolase family 18 (GH18). It has hydrolytic activity. Endoglycosidase F3 glycosylates α-1,6-fucosylated GlcNAc derivative to give natural, core fucosylated complex-type N-glycopeptides.

Packaging

Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5

Physical form

Aseptically filled solution in 20 mM Tris-HCl, pH 7.5

Other Notes

One unit will release N-linked oligosaccharides from 1 μmole of denatured porcine fibrinogen in 1 minute at 37 °C, pH 4.5.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000414802
0000451888
0000451888
0000414802
0000377143

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Chemical Biology of Glycoproteins (2017)
Advances in Carbohydrate Chemistry (2016)
Liwei Cao et al.
Nature communications, 13(1), 3910-3910 (2022-07-08)
Core fucosylation of N-linked glycoproteins has been linked to the functions of glycoproteins in physiological and pathological processes. However, quantitative characterization of core fucosylation remains challenging due to the complexity and heterogeneity of N-linked glycosylation. Here we report a mass
Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM
Ma J, et al.
Journal of proteomics, 189, 67-74 (2018)
Characterization of novel endo-beta-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
Huang Y, et al.
Scientific reports, 8(1), 246-246 (2018)
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Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

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