推荐产品
化驗
≥98.0% (HPLC)
形狀
powder
雜質
≤5% solvent (ethanol)
≤6% water
溶解度
H2O: 50 mg/mL, clear, colorless
儲存溫度
−20°C
SMILES 字串
[Na+].[Na+].OC[C@H]1O[C@@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2OC([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](O)[C@@H](O)[C@H]1O
InChI
1S/C15H24N2O17P2.2Na/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25;;/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25);;/q;2*+1/p-2/t5-,6-,8+,9-,10+,11-,12-,13?,14?;;/m1../s1
InChI 密鑰
PKJQEQVCYGYYMM-OUJOOSCPSA-L
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應用
Uridine 5dATP-diphosphogalactose (UDP-Gal) is a sugar-nucleotide substrate of galactosyltransferase(s) involved in the addition of galatose (galactosylation) molecules to N-linked and O-linked oligosaccharides and glycerolipids. UDP-Gal and its analogues are used to study the distribution, specificity and kinetics of galactosyltransferase(s).
儲存類別代碼
13 - Non Combustible Solids
水污染物質分類(WGK)
WGK 3
閃點(°F)
Not applicable
閃點(°C)
Not applicable
個人防護裝備
dust mask type N95 (US), Eyeshields, Gloves
Organic & biomolecular chemistry, 9(6), 1855-1863 (2011-01-27)
Structural analogues and mimics of the natural sugar-nucleotide UDP-galactose (UDP-Gal) are sought after as chemical tools for glycobiology and drug discovery. We have recently developed a novel class of galactosyltransferase (GalT) inhibitors derived from UDP-Gal, bearing an additional substituent at
Trends in plant science, 16(2), 98-107 (2010-12-15)
Galactoglycerolipids are the predominant lipid building blocks of chloroplast membranes and are essential for plant growth. Plant chloroplasts harbor a constitutive set of UDP-Gal-dependent lipid galactosyltransferases that are responsible for the bulk of galactoglycerolipid biosynthesis. A set of paralogs is
Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters.
Acta Biochimica Polonica, 58(3), 416-419 (2011)
Development of IgA nephropathy-like disease with high serum IgA levels and increased proportion of polymeric IgA in β-1,4-galactosyltransferase-deficient mice.
The American Journal of Pathology, 157, 125-128 (2007)
Biotechnology and bioengineering, 75(2), 239-251 (2001-09-06)
Variable N-glycosylation at Asn(297) in the Fc region of recombinant therapeutic immunoglobulin G (IgG) molecules, specifically terminal galactosylation and sialylation, may affect both pharmacokinetic behavior and effector functions of recombinant therapeutic antibodies. We investigated the hypothesis that IgG Fc glycosylation
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