GK80050- AdvanceBio β-N-acetylhexosaminidase (formerly ProZyme). Enzyme cleaves all nonreducing terminal β-linked N-acetylglucosamine (GlcNAc). Also known as N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. β(1-2,3,4,6)-specific. Use with GKX-5003 to determine the linkage position of β-linked GlcNAc residues. Does not release bisecting GlcNAc of N-glycans. No activity toward N-acetylgalactosamine (GalNAc). Includes 5x incubation buffer A [250 mM sodium phosphate pH 5.0].

Exoglycosidases

Доставка импортных компонентов по России от 3х недель транспортными компаниями СДЭК, Деловые Линии, Major Express.

Оплата физическими и юридическими лицами безналичным расчетом.

Цена может измениться после запроса у поставщика!

Артикул: GK80050 TME арт.: GK80050

Продавец

Технические характеристики

Concentration	40 U/mL
Enzyme Applications	Due to the complex nature of the specificity of this enzyme, it has been used extensively for the analysis of the positional isomerism of GlcNAc in glycans. It is complementary to the ß-N-acetylhexosaminidase from jack bean (GKX-5003).
Enzyme Formulation	20 mM Tris-HCl, 50 mM NaCl (pH 7.5)
Enzyme Source	Recombinant gene from Streptococcus pneumoniae, expressed in E. coli.
Enzyme Specificity	This enzyme releases nonreducing terminal ß(1-2,3,4, and 6)-linked N-acetylglucosamine from complex carbohydrates. When incubated with oligosaccharides at low concentrations (less than 50 mU/ml) the enzyme can differentiate between GlcNAcß1-2Man, GlcNAcß1-4Man and GlcNAcß1-6Man linkages. Under such conditions, the enzyme cleaves only ß1-2 linked GlcNAc, with two provisos. First, ß1-2 GlcNAc is not hydrolyzed if the mannose to which it is substituted has a substitution at C-6. Thus, the enzyme is useful for the analysis of triantennary oligosaccharides. Second, if the ß-linked mannose of the conserved pentasaccharide core is substituted with a ‘bisecting’ GlcNAc then only the ß1-2 linked GlcNAc linked to mannose on the a1-3 arm is cleaved. At higher concentrations of the enzyme, ß(1-4) and ß(1-6)-linked GlcNAc may also be hydrolyzed. The reported activity against O-linked oligosaccharides suggests that GlcNAc ß1-3Gal and GlcNAc ß1-6Gal are digested1. Although the specificity towards oligosaccharides containing GalNAc is not known, the enzyme, in common with other glucosaminidases, also hydrolyses pNP-ß-GalNAc at pH 6.0 and 37C. The activity towards this substrate is ~7 fold less than towards pNP-ßGlcNAc.
Enzyme Unit Definition	One unit is defined as the amount of enzyme required to catalyze the release of 1 mole of p-nitrophenol from p-nitrophenol-N-acetyl-ß-D-glucosaminide per minute at 37C, pH 5.0
Unit	1.6 U
Volume	40 µL
pH Optimum	5