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U5252

Sigma-Aldrich

Uridine 5′-diphospho-N-acetylgalactosamine disodium salt

≥97%

Synonym(s):

(UDP)-GalNAc, UDP-GalNAc, UDP-N-acetylgalactosamine, Uridine[5′]diphospho[1](2-acetamino-2-deoxy-α-D-galactopyranose) disodium salt

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About This Item

Empirical Formula (Hill Notation):
C17H25N3Na2O17P2
CAS Number:
108320-87-2
Molecular Weight:
651.32
Beilstein:
5375867
MDL number:
MFCD00077894
UNSPSC Code:
41106305
PubChem Substance ID:
24900653
NACRES:
NA.51

biological source

synthetic (organic)

Quality Level

200

Assay

≥97%

form

powder

storage temp.

−20°C

SMILES string

[Na+].[Na+].CC(=O)N[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OP([O-])(=O)OP([O-])(=O)OC[C@H]2OC([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O

InChI

1S/C17H27N3O17P2.2Na/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28;;/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28);;/q;2*+1/p-2/t7-,8-,10-,11+,12-,13-,14-,15?,16?;;/m1../s1

InChI key

HXWKMJZFIJNGES-QCVFHWOISA-L

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General description

Uridine diphosphate (UDP)-GalNAc acts as a precursor in the biosynthesis of O-linked oligosaccharide. It also acts as a substrate for synthesis of chitin, a vital element of cell walls in fungi and of exoskeletons of arthropods and insects.

Application

Uridine 5′-diphospho-N-acetylgalactosamine disodium salt has been used as a substrate for polypeptide N-acetylgalactosaminyltransferase (ppGalNAc-T).

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Daniel R Evans et al.
Human mutation, 39(8), 1092-1101 (2018-05-12)
Characterizing moderate penetrance susceptibility genes is an emerging frontier in colorectal cancer (CRC) research. GALNT12 is a strong candidate CRC-susceptibility gene given previous linkage and association studies, and inactivating somatic and germline alleles in CRC patients. Previously, we found rare
Anthony P Corfield
Microorganisms, 6(3) (2018-08-04)
Glycoproteins are major players in the mucus protective barrier in the gastrointestinal and other mucosal surfaces. In particular the mucus glycoproteins, or mucins, are responsible for the protective gel barrier. They are characterized by their high carbohydrate content, present in
Hongwei Wu et al.
Nucleic acids research, 33(9), 2822-2837 (2005-05-20)
We present a computational method for the prediction of functional modules encoded in microbial genomes. In this work, we have also developed a formal measure to quantify the degree of consistency between the predicted and the known modules, and have
Earnest James Paul Daniel et al.
Glycobiology, 30(11), 910-922 (2020-04-19)
A family of polypeptide GalNAc-transferases (GalNAc-Ts) initiates mucin-type O-glycosylation, transferring GalNAc onto hydroxyl groups of Ser and Thr residues of target substrates. The 20 GalNAc-T isoenzymes in humans are classified into nine subfamilies according to sequence similarity. GalNAc-Ts select their
Inhibitor of ppGalNAc-T3-mediated O-glycosylation blocks cancer cell invasiveness and lowers FGF23 levels
Song L and Linstedt AD
eLife, 6, e24051-e24051 (2017)
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The presence of multiple functional groups and stereocenters in complex carbohydrates makes them challenging targets for the organic chemist.

Glycosyltransferases

Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the one enzyme-one linkage concept. Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some nucleoside mono- or diphosphate sugar donors.

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