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

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

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

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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

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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