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E2264
Endoglycosidase F3 from Elizabethkingia miricola
recombinant, expressed in E. coli, 30 U/mg
Synonym(e):
Elizabethkingia miricola, Endo-β-N-acetylglucosaminidase F3, Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum
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About This Item
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Konjugat
(N-linked)
Form
solution
Spezifische Aktivität
30 U/mg
Mol-Gew.
32 kDa
Versandbedingung
wet ice
Lagertemp.
2-8°C
Anwendung
Endoglycosidase F3 from Elizabethkingia miricola has been used to analyze core fucosylation and tryptic digests of serum proteins.
Biochem./physiol. Wirkung
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.
Verpackung
Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5
Einheitendefinition
One unit will release N-linked oligosaccharides from 1 μmole of denatured porcine fibrinogen in 1 minute at 37 °C, pH 4.5.
Physikalische Form
Aseptically filled solution in 20 mM Tris-HCl, pH 7.5
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
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
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