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A2795

Sigma-Aldrich

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:
1811-31-0
Molecular Weight:
221.21
Beilstein/REAXYS Number:
2331340
EC Number:
217-321-9
MDL number:
MFCD00065372
UNSPSC Code:
12352201
PubChem Substance ID:
24890693
NACRES:
NA.25

Quality Level

300

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

InChI key

OVRNDRQMDRJTHS-KEWYIRBNSA-N

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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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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P Van den Steen et al.
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
Sian F Irvine et al.
International journal of molecular sciences, 19(4) (2018-04-13)
Perineuronal nets (PNNs) are extracellular matrix structures surrounding neuronal sub-populations throughout the central nervous system, regulating plasticity. Enzymatically removing PNNs successfully enhances plasticity and thus functional recovery, particularly in spinal cord injury models. While PNNs within various brain regions are
Yuki Kuramoto et al.
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
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
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)
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