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E9762

Sigma-Aldrich

Endoglycosidase F1 from Elizabethkingia miricola

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

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Synonym(s):
Endo F1, Endo-β-N-acetylglucosaminidase F1, Endoglycosidase F1 from Chryseobacterium meningosepticum, Endoglycosidase F1 from Elizabethkingia meningoseptica, Endoglycosidase F1 from Flavobacterium meningosepticum
Enzyme Commission number:
MDL number:
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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This Item
E0639E2264A0810
form

buffered aqueous solution

form

solution

form

solution

form

buffered aqueous solution

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

mol wt

32 kDa

mol wt

32 kDa

mol wt

32 kDa

mol wt

-

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

Storage Class

12 - Non 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)


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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)
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)
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)
Helena Ryšlavá et al.
The FEBS journal, 278(14), 2469-2484 (2011-05-14)
Fungal β-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group

Articles

Explore various strategies for deglycosylating N-linked glycans involving PNGase F, PNGase A (Glycopeptidase A), and even native and sequential deglycosylation with endoglycosidases like Endoglycosidase H, Endoglycosidase F, and exoglycosidases.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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