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MilliporeSigma

E9762

Sigma-Aldrich

Endoglycosidase F1

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

Sinónimos:

Endoglycosidase F1, Endoglycosidase F1 from Elizabethkingia meningoseptica

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About This Item

Comisión internacional de enzimas:
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

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)


Certificados de análisis (COA)

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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)
Roger S Zou et al.
Aging, 3(10), 968-984 (2011-10-13)
A distinct conformational transition from the α-helix-rich cellular prion protein (PrPC) into its β-sheet-rich pathological isoform (PrPSc) is the hallmark of prion diseases, a group of fatal transmissible encephalopathies that includes spontaneous and acquired forms. Recently, a PrPSc-like intermediate form

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