E2264
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
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32
Recommended Products
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
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 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)
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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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