U1881
Uridine 5′-diphosphoglucose-[glucose-6-3H] ammonium salt
aqueous ethanol solution
Sinónimos:
UDP-Glucose, UDP-glc, UDPG
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About This Item
Fórmula lineal:
C15H22N2O17P2 · NH3
Número de CAS:
Peso molecular:
581.32
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
form
aqueous ethanol solution
extent of labeling
3-10 Ci/mmol
shipped in
dry ice
storage temp.
−20°C
SMILES string
N.[H]C(O)C1OC(OP(O)(=O)OP(O)(=O)OCC2OC(C(O)C2O)N3C=CC(=O)NC3=O)C(O)C(O)C1O
Physical form
Ethanol: water (1:1) solution
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Jeffrey A Gross et al.
BMC genomics, 16, 672-672 (2015-09-04)
The recent discovery that methylated cytosines are converted to 5-hydroxymethylated cytosines (5hmC) by the family of ten-eleven translocation enzymes has sparked significant interest on the genomic location, the abundance in different tissues, the putative functions, and the stability of this
Hiroshi Fukayama et al.
Bioscience, biotechnology, and biochemistry, 78(4), 609-613 (2014-07-19)
Phosphoenolpyruvate carboxylase (PEPC) undergoes activity regulation through reversible phosphorylation. The day/night phosphorylation of leaf PEPC in 27 C3 plant species was analyzed by immunoblotting. PEPC was phosphorylated in the daytime in 12 species, whereas it was phosphorylated at night in
Susannah M L Gagnon et al.
The Journal of biological chemistry, 290(45), 27040-27052 (2015-09-17)
Homologous glycosyltransferases α-(1→3)-N-acetylgalactosaminyltransferase (GTA) and α-(1→3)-galactosyltransferase (GTB) catalyze the final step in ABO(H) blood group A and B antigen synthesis through sugar transfer from activated donor to the H antigen acceptor. These enzymes have a GT-A fold type with characteristic
Robyn Meech et al.
Molecular pharmacology, 87(3), 442-450 (2014-12-19)
The human UDP glycosyltransferase (UGT) superfamily comprises four families of enzymes that catalyze the addition of sugar residues to small lipophilic chemicals. The UGT1 and UGT2 enzymes use UDP-glucuronic acid, and UGT3 enzymes use UDP-N-acetylglucosamine, UDP-glucose, and UDP-xylose to conjugate
Karen M J Saerens et al.
FEMS yeast research, 15(7) (2015-08-25)
Altering glycolipid structure by genetic engineering of Starmerella bombicola is a recently started research topic and worthy alternative to the unsuccessful selective feeding strategies conventionally applied to reach this goal. One question to be addressed when expressing heterologous proteins in
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