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G7000

Sigma-Aldrich

α-D-Glucose 1-phosphate disodium salt hydrate

≥97% (Enzymatic Purity, anhydrous)

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Synonym(s):
α-D-Glucopyranose 1-phosphate, Cori ester
Linear Formula:
C6H11O9PNa2 · xH2O
CAS Number:
Molecular Weight:
304.10 (anhydrous basis)
EC Number:
MDL number:
PubChem Substance ID:
NACRES:
NA.25

biological source

synthetic

Quality Level

assay

≥97% (Enzymatic Purity, anhydrous)

form

powder

impurities

≤0.1 mol % glucose
≤0.5 mol % α-D-glucose 1,6-diphosphate

color

white

solubility

water: 50 mg/mL, clear, colorless

cation traces

Na: 13.5-16.7% (anhydrous)

application(s)

agriculture

storage temp.

−20°C

SMILES string

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

InChI

1S/C6H13O9P.2Na.H2O/c7-1-2-3(8)4(9)5(10)6(14-2)15-16(11,12)13;;;/h2-10H,1H2,(H2,11,12,13);;;1H2/q;2*+1;/p-2/t2-,3-,4+,5-,6-;;;/m1.../s1

InChI key

YWAUQXHOCBBYLP-FBNUBEQJSA-L

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G6875G6750G7250
vibrant-m

G6750

α-D-Glucose 1-phosphate dipotassium salt hydrate

Premium Grade
Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

300

biological source

synthetic

biological source

synthetic

biological source

synthetic

biological source

synthetic (organic)

assay

≥97% (Enzymatic Purity, anhydrous)

assay

≥97% (HPLC)

assay

≥99% (HPLC)

assay

≥98% (HPLC)

impurities

≤0.1 mol % glucose, ≤0.5 mol % α-D-glucose 1,6-diphosphate

impurities

glucose, essentially free

impurities

glucose and starch, essentially free

impurities

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

α-D-Glucose 1-phosphate is converted into D-glucose-6-phosphate by the enzyme phosphoglucomutase.

Biochem/physiol Actions

Glucose-1-phosphate (G1P) is produced from glycogen during glycogenolysis by the actions of glycogen phosphorylase. Conversion to glucose-6-phosphate (G6P) by phosphoglucomutase allows for entry of the glucose molecule into metabolic pathways such as glycolysis. During glycogenesis, G6P is converted to G1P by the actions of phosphoglucose isomerase.

Preparation Note

Prepared by a modification of the procedure of McCready, R.M., et al., J. Am. Chem. Soc., 66, 560 (1944).

Other Notes

To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Rickard Olsson et al.
Environmental science & technology, 46(1), 285-291 (2011-11-23)
Esters of phosphoric acid constitute a sizable fraction of the total phosphorus supply in the environment and thus play an important role in the global phosphorus cycle. Enzymatic hydrolysis of these esters to produce orthophosphate is often a required reaction
Fumiaki Ito et al.
Biochimica et biophysica acta, 1844(4), 759-766 (2014-02-05)
The archaeal non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN, EC 1.2.1.9) is a highly allosteric enzyme activated by glucose 1-phosphate (Glc1P). Recent kinetic analyses of two GAPN homologs from Sulfolobales show different allosteric behaviors toward the substrate glyceraldehyde-3-phosphate (GAP) and the allosteric effector
Rickard Olsson et al.
Langmuir : the ACS journal of surfaces and colloids, 26(24), 18760-18770 (2010-11-20)
Adsorption, desorption, and precipitation reactions at environmental interfaces govern the fate of phosphorus in terrestrial and aquatic environments. Typically, a substantial part of the total pool of phosphorus consists of organophosphate, and in this study we have focused on the
Cátia Nunes et al.
Plant physiology and biochemistry : PPB, 63, 89-98 (2012-12-22)
SnRK1 of the SNF1/AMPK group of protein kinases is an important regulatory protein kinase in plants. SnRK1 was recently shown as a target of the sugar signal, trehalose 6-phosphate (T6P). Glucose 6-phosphate (G6P) can also inhibit SnRK1 and given the
Jelena Ciric et al.
Carbohydrate polymers, 93(1), 31-37 (2013-03-08)
An in vitro enzyme-catalyzed tandem reaction using the enzymes phosphorylase b from rabbit muscle and Deinococcus geothermalis glycogen branching enzyme (Dg GBE) to obtain branched polyglucans with tunable degree of branching (2% ÷ 13%) is presented. The tunable degree of

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