A2795
N-Acetyl-D-galactosamine
≥98% (HPLC)
Synonym(s):
2-Acetamido-2-deoxy-D-galactose, D-GalNAc, N-Acetylchondrosamine
Sign Into View Organizational & Contract Pricing
All Photos(1)
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
InChI key
OVRNDRQMDRJTHS-KEWYIRBNSA-N
Looking for similar products? Visit Product Comparison Guide
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
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service