UDP-Alpha-d-n-acetylgalactosamine, disodium salt

Names

[ Name ]:
UDP-Alpha-d-n-acetylgalactosamine, disodium salt

[Synonym ]:
UDP-N-acetylgalactosamine
Uridine 5'-diphospho-N-acetylgalactosamine sodium salt
MFCD00077894
Uridine 5'-diphospho-N-acetylgalactosamine disodium salt
Uridine 5 inverted exclamation marka-diphospho-N-acetylgalactosamine disodium salt
Uridine 5'-(trihydrogen diphosphate) P'-[2-(acetylamino)-2-deoxy-alpha-D-galactopyranosyl] ester disodium salt
UDP-Alpha-d-n-acetylgalactosamine, disodium salt

Biological Activity

[Description]:

UDP-GalNAc (UDP-N-acetyl-D-galactosamine) disodium is a sugar nucleotide and a substrate of EpsC115. EpsC115 is an exopolymeric substances (EPS) N-terminal deletion mutant with the residue 1-115 deletion. UDP-GalNAc UDP-GalNAc is the donor substrate of many N-acetylgalactosaminyltransferases, enzymes which transfer GalNAc from the nucleotide sugar to a saccharide or peptide acceptor[1].

[Related Catalog]:

Research Areas >> Metabolic Disease

[References]

[1]. Kaundinya CR, et al. In vitro characterization of N-terminal truncated EpsC from Bacillus subtilis 168, a UDP-N-acetylglucosamine 4,6-dehydratase. Arch Biochem Biophys. 2018 Nov 1;657:78-88.

[2]. Hang HC, et al. Probing glycosyltransferase activities with the Staudinger ligation. J Am Chem Soc. 2004 Jan 14;126(1):6-7.

Chemical & Physical Properties

[ Molecular Formula ]:
C₁₇H₂₅N₃Na₂O₁₇P₂

[ Molecular Weight ]:
651.31700

[ Exact Mass ]:
651.04500

[ PSA ]:
331.14000

[ Storage condition ]:
−20°C

[ Water Solubility ]:
H2O: 50 mg/mL, clear, colorless

MSDS

Click to get detail MSDS

Safety Information

[ Personal Protective Equipment ]:
dust mask type N95 (US);Eyeshields;Gloves

[ Hazard Codes ]:
Xi: Irritant;

[ Risk Phrases ]:
36/37/38

[ Safety Phrases ]:
26-36

[ RIDADR ]:
NONH for all modes of transport

[ WGK Germany ]:
3

Synthetic Route

Click to get detail synthetic route

Precursor & DownStream

Precursor

DownStream

Articles

Expression of the functional recombinant human glycosyltransferase GalNAcT2 in Escherichia coli.

Microb. Cell Fact. 14 , 3, (2015)

Recombinant protein-based therapeutics have become indispensable for the treatment of many diseases. They are produced using well-established expression systems based on bacteria, yeast, insect and ma...

Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy.

PLoS ONE 9(2) , e99026, (2014)

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-acetylneurami...

Prediction of functional modules based on comparative genome analysis and Gene Ontology application.

Nucleic Acids Res. 33 , 2822-37, (2005)

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 bet...