Skip to Content
Merck
All Photos(2)

Key Documents

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

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

synthetic (organic)

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

Looking for similar products? Visit Product Comparison Guide

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)

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.

Visit the Document Library

Kazuo Takahashi et al.
PloS one, 9(2), e99026-e99026 (2014-06-12)
Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). We have analyzed O-glycosylation heterogeneity of naturally asialo-IgA1 (Ale) myeloma protein that mimics Gal-deficient
Amanda Fritzen et al.
PLoS neglected tropical diseases, 12(7), e0006598-e0006598 (2018-07-10)
Crimean-Congo hemorrhagic fever virus (CCHFV) causes severe acute human disease with lethal outcome. The knowledge about the immune response for this human health threat is highly limited. In this study, we have screened the glycoprotein of CCHFV for novel linear
Expression of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase isozymes T1 and T2 in human colorectal cancer
Kohsaki T, et al.
Journal of Gastroenterology, 35(11), 840-848 (2000)
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
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

Articles

Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.

LC-MS/MS method quantifies similar polar nucleotide activated sugars using Supel™ Carbon LC column for simultaneous analysis.

Enzymatic glycosyltransferase specificity challenges the one enzyme-one linkage concept.

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