E2264
Endoglycosidase F3 from Elizabethkingia miricola
recombinant, expressed in E. coli, 30 U/mg
Sinónimos:
Elizabethkingia miricola, Endo-β-N-acetylglucosaminidase F3, Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum
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About This Item
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32
Productos recomendados
recombinant
expressed in E. coli
Quality Level
conjugate
(N-linked)
form
solution
specific activity
30 U/mg
mol wt
32 kDa
shipped in
wet ice
storage temp.
2-8°C
Categorías relacionadas
Application
Endoglycosidase F3 from Elizabethkingia miricola has been used to analyze core fucosylation and tryptic digests of serum proteins.
Biochem/physiol Actions
Cleaves asparagine-linked biantennary and triantennary complex, oligosaccharides depending on the state of core fucosylation and peptide linkage.
Endoglycosidase F3 belongs to the glycoside hydrolase family 18 (GH18). It has hydrolytic activity. Endoglycosidase F3 glycosylates α-1,6-fucosylated GlcNAc derivative to give natural, core fucosylated complex-type N-glycopeptides.
Packaging
Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5
Unit Definition
One unit will release N-linked oligosaccharides from 1 μmole of denatured porcine fibrinogen in 1 minute at 37 °C, pH 4.5.
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)
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Characterization of novel endo-beta-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
Huang Y, et al.
Scientific reports, 8(1), 246-246 (2018)
Chemical Biology of Glycoproteins (2017)
Advances in Carbohydrate Chemistry (2016)
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)
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
Artículos
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