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Merck

U5252

Sigma-Aldrich

Uridine 5′-diphospho-N-acetylgalactosamine disodium salt

≥97%

Synonim(y):

(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

Wzór empiryczny (zapis Hilla):
C17H25N3Na2O17P2
Numer CAS:
Masa cząsteczkowa:
651.32
Beilstein:
5375867
Numer MDL:
Kod UNSPSC:
41106305
Identyfikator substancji w PubChem:
NACRES:
NA.51

pochodzenie biologiczne

synthetic (organic)

Próba

≥97%

Postać

powder

temp. przechowywania

−20°C

ciąg SMILES

[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

Klucz InChI

HXWKMJZFIJNGES-QCVFHWOISA-L

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Opis ogólny

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.

Zastosowanie

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

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Środki ochrony indywidualnej

dust mask type N95 (US), Eyeshields, Gloves


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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)

Produkty

The presence of multiple functional groups and stereocenters in complex carbohydrates makes them challenging targets for the organic chemist.

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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