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About This Item
Specific activity:
≥16 U/mg
Recombinant:
expressed in E. coli
Product Name
Endoglycosidase F1 from Elizabethkingia miricola, recombinant, expressed in E. coli, ≥16 U/mg, buffered aqueous solution
recombinant
expressed in E. coli
conjugate
(N-linked)
form
buffered aqueous solution
specific activity
≥16 U/mg
mol wt
32 kDa
shipped in
wet ice
storage temp.
2-8°C
Quality Level
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General description
Endoglycosidase F1 from Elizabethkingia miricola is a glycan specific enzyme.
Application
Cleaves asparagine-linked or free oligomannose and hybrid, but not complex, oligosaccharides.
Endoglycosidase F1 from Elizabethkingia miricola has been used to remove binding of human hemochromatosis protein (HFE) to cation independent mannose-6-phosphate receptor (CI-MPR) and to glycosylate fucosylated N-glycopeptides.
Biochem/physiol Actions
Endoglycosidase F1 from Elizabethkingia miricola plays an important role in cleavage of glycan structures from the protein by cleaving between the two N-acetylglucosamine residues of the chitobiose core. It mediates high mannose and hybrid oligosaccharides cleavage.
Packaging
Supplied with 5× Reaction Buffer, 250 mM NaH2PO4, pH 5.5.
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 Ribonuclease B in 1 minute at 37 °C, pH 5.5.
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Receptor activity-modifying protein 1 determines the species selectivity of non-peptide CGRP receptor antagonists
Mallee JJ, et al.
The Journal of Biological Chemistry, 277, 14294-14298 (2002)
EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and alpha-acid glycoprotein
Jonathan S, et al.
BioChemistry: An Indian Journal, 455, 107-118 (2013)
In vitro binding of HFE to the cation-independent mannose-6 phosphate receptor
Schimanski LM, et al.
Blood Cells, Molecules and Diseases, 43(2), 180-193 (2009)
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)
Yusuke Tomabechi et al.
Carbohydrate research, 345(17), 2458-2463 (2010-10-12)
To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-β-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to
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