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U5252

Sigma-Aldrich

Uridine 5′-diphospho-N-acetylgalactosamine disodium salt

≥97%

Sinónimos:

UDP-N-acetylgalactosamine

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About This Item

Fórmula empírica (notación de Hill):
C17H25N3Na2O17P2
Número de CAS:
108320-87-2
Peso molecular:
651.32
Beilstein/REAXYS Number:
5375867
MDL number:
MFCD00077894
UNSPSC Code:
41106305
PubChem Substance ID:
24900653
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

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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

11 - Combustible Solids

wgk_germany

WGK 3

ppe

dust mask type N95 (US), Eyeshields, Gloves

Certificados de análisis (COA)

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Xiaofei Guo et al.
Animals : an open access journal from MDPI, 8(10) (2018-09-23)
A new fecundity gene named the FecL (mutation), which regulates the ovulation rate, was discovered in French Lacaune sheep. The B4GALNT2 (beta-1, 4-N-acetyl-galactosaminyl transferase 2) gene was considered as the potential FecL mutation gene. This study explores whether the effect
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
UDP-sugar producing pyrophosphorylases--distinct and essential enzymes with overlapping substrate specificities, providing de novo precursors for glycosylation reactions
Decker D and Kleczkowski LA
Frontiers in Plant Science, 9, 1822-1822 (2018)
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)
Erandi Lira-Navarrete et al.
Nature communications, 6, 6937-6937 (2015-05-06)
Protein O-glycosylation is controlled by polypeptide GalNAc-transferases (GalNAc-Ts) that uniquely feature both a catalytic and lectin domain. The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and catalysis remains unclear. Here we present the
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