A2795
N-Acetyl-D-galactosamine
≥98% (HPLC)
Synonym(s):
2-Acetamido-2-deoxy-D-galactose, D-GalNAc, N-Acetylchondrosamine
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About This Item
Empirical Formula (Hill Notation):
C8H15NO6
CAS Number:
Molecular Weight:
221.21
Beilstein:
2331340
EC Number:
MDL number:
UNSPSC Code:
12352201
PubChem Substance ID:
NACRES:
NA.25
Recommended Products
Quality Level
Assay
≥98% (HPLC)
form
powder
technique(s)
HPLC: suitable
color
white
mp
160 °C
solubility
water: 50 mg/mL, clear, colorless
storage temp.
2-8°C
SMILES string
CC(=O)N[C@H]1C(O)O[C@H](CO)[C@H](O)[C@@H]1O
InChI
1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6+,7-,8?/m1/s1
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General description
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Dezemon Zingue et al.
Scientific reports, 8(1), 6778-6778 (2018-05-02)
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
David J Gill et al.
Trends in cell biology, 21(3), 149-158 (2010-12-15)
O-GalNAc glycosylation of proteins confers essential structural, protective and signaling roles in eumetazoans. Addition of O-glycans onto proteins is an extremely complex process that regulates both sites of attachment and the types of oligosaccharides added. Twenty distinct polypeptide GalNAc-transferases (GalNAc-Ts)
Ju Huang et al.
Molecular therapy. Methods & clinical development, 5, 241-258 (2017-06-13)
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
Malte Lenders et al.
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
Karineh Petrossian et al.
Acta histochemica, 109(6), 491-500 (2007-08-21)
By using a non-cancer and a cancer cell line originally from the same tissue (colon), coupled with testing lectins for cell binding and for their effects on these cell lines in culture, this study describes a simple multi-parameter approach that
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