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A4394

Sigma-Aldrich

N-Acetyl-D-glucosamine 6-phosphate sodium salt

≥98% (TLC)

Synonym(s):

GlcNAc-6-P Sodium Salt

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About This Item

Empirical Formula (Hill Notation):
C8H16NO9P · xNa+
Molecular Weight:
301.19 (free acid basis)
MDL number:
MFCD00057520
UNSPSC Code:
12352201
PubChem Substance ID:
24890856
NACRES:
NA.25

biological source

natural (inorganic)

Quality Level

200

assay

≥98% (TLC)

form

powder

technique(s)

thin layer chromatography (TLC): suitable

impurities

<10% water (Karl Fischer)

color

white to light yellow

solubility

water: 50 mg/mL, clear, colorless

storage temp.

−20°C

SMILES string

[Na].CC(=O)NC1C(O)OC(COP(O)(O)=O)C(O)C1O

InChI

1S/C8H16NO9P.Na.H/c1-3(10)9-5-7(12)6(11)4(18-8(5)13)2-17-19(14,15)16;;/h4-8,11-13H,2H2,1H3,(H,9,10)(H2,14,15,16);;

InChI key

AILBPHCGSZBCSM-UHFFFAOYSA-N

Related Categories

Application

N-Acetyl-D-glucosamine 6-phosphate (GlcNAc-6P), an intracellular form of GlcNAc, is a substrate used to identify, differentiate and characterize N-acetyl-D-glucosamine-phosphate deacetylase(s).

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.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

ppe

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Tim Miyashiro et al.
Molecular microbiology, 82(4), 894-903 (2011-10-14)
To successfully colonize and persist within a host niche, bacteria must properly regulate their gene expression profiles. The marine bacterium Vibrio fischeri establishes a mutualistic symbiosis within the light organ of the Hawaiian squid, Euprymna scolopes. Here, we show that
Richard S Hall et al.
Biochemistry, 46(27), 7953-7962 (2007-06-15)
NagA catalyzes the hydrolysis of N-acetyl-d-glucosamine-6-phosphate to d-glucosamine-6-phosphate and acetate. X-ray crystal structures of NagA from Escherichia coli were determined to establish the number and ligation scheme for the binding of zinc to the active site and to elucidate the
Richard S Hall et al.
Biochemistry, 46(27), 7942-7952 (2007-06-15)
NagA is a member of the amidohydrolase superfamily and catalyzes the deacetylation of N-acetyl-d-glucosamine-6-phosphate. The catalytic mechanism of this enzyme was addressed by the characterization of the catalytic properties of metal-substituted derivatives of NagA from Escherichia coli with a variety
Juan Wang et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 62(Pt 11), 1097-1099 (2006-11-02)
Glucosamine-6-phosphate N-acetyltransferase from human liver, which catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amine of D-glucosamine 6-phosphate to form N-acetyl-D-glucosamine 6-phosphate, was expressed in a soluble form from Escherichia coli strain BL21

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