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U4625

Sigma-Aldrich

Uridine 5′-diphosphoglucose disodium salt hydrate from Saccharomyces cerevisiae

≥98%

Synonym(s):

UDP-Glc hydrate, UDPG hydrate

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About This Item

Empirical Formula (Hill Notation):
C15H22N2Na2O17P2 · xH2O
CAS Number:
Molecular Weight:
610.27 (anhydrous basis)
MDL number:
UNSPSC Code:
41106305
PubChem Substance ID:
NACRES:
NA.51

biological source

Saccharomyces cerevisiae

Quality Level

assay

≥98%

form

powder

storage temp.

−20°C

SMILES string

O.[Na+].[Na+].OC[C@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](O)[C@@H](O)[C@@H]1O

InChI

1S/C15H24N2O17P2.2Na.H2O/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);;;1H2/q;2*+1;/p-2/t5-,6-,8-,9-,10+,11-,12-,13-,14-;;;/m1.../s1

InChI key

SRHFBUUOPANXBG-WSIJJEQHSA-L

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General description

Uridine diphosphate glucose (UDP-glucose) is a glycogen precursor. The transfer of glucose from UDP-glucose to growing glycogen chain is catalyzed by the enzyme glycogen synthase. The enzyme uridine diphosphate galactose-4-epimerase catalyzes the formation of UDP-glucose from UDP-galactose.

Application

Uridine 5′-diphosphoglucose disodium salt hydrate from Saccharomyces cerevisiae has been used as a substrate
  • for the PpIRX10 enzyme activity from Arabidopsis thaliana
  • in radiometric assay of glycosyltransferases (GTs)
  • in uridine diphosphate glucose (UDP-Glc) 4-epimerase assay in Arabidopsis thaliana samples

Biochem/physiol Actions

Uridine diphosphate glucose (UDP-glucose) is an essential mediator of the cellular metabolic pathways. In yeast, the high levels of trehalose and glycogen favor increased levels of UDP-glucose.

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Distinct properties of the five UDP-D-glucose/UDP-D-galactose 4-epimerase isoforms of Arabidopsis thaliana
Barber C, et al.
The Journal of Biological Chemistry, 281(25), 17276-17285 (2006)
Hypoglycemia as a Pathological Result in Medical Praxis
Type 1 Diabetes Complications (2011)
A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism
Fuhring J, et al.
Scientific Reports, 5, 9618-9618 (2015)
Radiometric and spectrophotometric in vitro assays of glycosyltransferases involved in plant cell wall carbohydrate biosynthesis
Brown C, et al.
Nature Protocols, 7(9), 1634-1634 (2012)
Unravelling evolutionary strategies of yeast for improving galactose utilization through integrated systems level analysis
Hong KK, et al.
Proceedings of the National Academy of Sciences of the USA, 108(29), 12179-12184 (2011)

Articles

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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