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
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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 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)
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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
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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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