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E9762

Sigma-Aldrich

Endoglycosidase F1 from Elizabethkingia miricola

recombinant, expressed in E. coli, ≥16 U/mg, buffered aqueous solution

Synonym(s):

Endo F1, Endo-β-N-acetylglucosaminidase F1, Endoglycosidase F1 from Chryseobacterium meningosepticum, Endoglycosidase F1 from Elizabethkingia meningoseptica, Endoglycosidase F1 from 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

buffered aqueous solution

specific activity

≥16 U/mg

mol wt

32 kDa

shipped in

wet ice

storage temp.

2-8°C

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General description

Endoglycosidase F1 from Elizabethkingia miricola is a glycan specific enzyme.

Application

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.
Cleaves asparagine-linked or free oligomannose and hybrid, but not complex, oligosaccharides.

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.

Unit Definition

One unit will release N-linked oligosaccharides from 1 μmole of denatured Ribonuclease B in 1 minute at 37 °C, pH 5.5.

Physical form

Aseptically filled solution in 20 mM Tris-HCl pH 7.5

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

常规特殊物品

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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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)
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)
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)
Liv Anette Bøhle et al.
FEMS microbiology letters, 325(2), 123-129 (2011-11-19)
It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18 endoglycosidase domain and a GH20 domain.

Articles

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

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