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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

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

conjugate

(N-linked)

form

solution

specific activity

30 U/mg

mol wt

32 kDa

shipped in

wet ice

storage temp.

2-8°C

Application

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

Biochem/physiol Actions

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.
Cleaves asparagine-linked biantennary and triantennary complex, oligosaccharides depending on the state of core fucosylation and peptide linkage.

Packaging

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

Unit Definition

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

Physical form

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

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Advances in Carbohydrate Chemistry (2016)
Chemical Biology of Glycoproteins (2017)
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)
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)

Articles

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

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

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

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

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