N-Acetyl-D-galactosamine (GalNAc), an amino sugar, is a component of many O-linked and N-linked glycan structures. As uridine diphosphate (UDP)-GalNAc, GalNAc is the initial O-linked sugar to many serine and threonine residues in protein glycosylations.
Application
N-Acetyl-D-galactosamine has been used:
as a Dolichos biflorus agglutinin (DBA) haptenic sugar in lectin bead binding assay
to assess the specificity of lectin binding using lectin blot inhibition
in immunohistochemistry to pre-adsorb Wisteria floribunda lectin
N-Acetyl-D-galactosamine (GalNAc), an aminosugar, is a component of many O-linked and N-linked glycan structures. As UDP-GalNAc, GalNAc is the intial O-linked sugar to many serine and threonine residues in protein glycosylations.
Other Notes
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association, 32(12), 2090-2097 (2016-09-30)
Renal and cardiac involvement is responsible for substantial morbidity and mortality in Fabry disease (FD). We analysed the incidence of FD-related renal, cardiac and neurologic end points in patients with FD on long-term enzyme replacement therapy (ERT). A retrospective analysis
Journal of molecular and cellular cardiology, 121, 256-265 (2018-07-27)
Fabry disease is an X-linked disease caused by mutations in α-galactosidase A (GLA); these mutations result in the accumulation of its substrates, mainly globotriaosylceramide (Gb3). The accumulation of glycosphingolipids induces pathogenic changes in various organs, including the heart, and Fabry
Critical reviews in biochemistry and molecular biology, 33(3), 151-208 (1998-07-23)
The biosynthesis, structures, and functions of O-glycosylation, as a complex posttranslational event, is reviewed and compared for the various types of O-glycans. Mucin-type O-glycosylation is initiated by tissue-specific addition of a GalNAc-residue to a serine or a threonine of the
Contaminations and fastidiousness of M. ulcerans may have both hamper isolation of strains from environmental sources. We aimed to optimize decontamination and culture of environmental samples to circumvent both limitations. Three strains of M. ulcerans cultured onto Middlebrook 7H10 at
Fabry disease is a rare lysosomal storage disorder (LSD). We designed multiple recombinant lentivirus vectors (LVs) and tested their ability to engineer expression of human α-galactosidase A (α-gal A) in transduced Fabry patient CD34
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