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
Looking for similar products? Visit Product Comparison Guide
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.
General description
Endoglycosidase F1 from Elizabethkingia miricola is a glycan specific enzyme.
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.
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
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)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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)
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
Related Content
Instructions
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service