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A4394

Sigma-Aldrich

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

≥98% (TLC)

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About This Item

Empirische Formel (Hill-System):
C8H16NO9P · xNa+
Molekulargewicht:
301.19 (free acid basis)
MDL-Nummer:
MFCD00057520
UNSPSC-Code:
12352201
PubChem Substanz-ID:
24890856
NACRES:
NA.25

Biologische Quelle

natural (inorganic)

Qualitätsniveau

200

Assay

≥98% (TLC)

Form

powder

Methode(n)

thin layer chromatography (TLC): suitable

Verunreinigungen

<10% water (Karl Fischer)

Farbe

white to light yellow

Löslichkeit

water: 50 mg/mL, clear, colorless

Lagertemp.

−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);;

InChIKey

AILBPHCGSZBCSM-UHFFFAOYSA-N

Verwandte Kategorien

Anwendung

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).

Sonstige Hinweise

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

Piktogramme

Exclamation mark
GHS07

Signalwort

Warning

Gefahreneinstufungen

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

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Persönliche Schutzausrüstung

dust mask type N95 (US), Eyeshields, Gloves

Analysenzertifikate (COA)

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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
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
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
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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