추천 제품
생물학적 소스
natural (inorganic)
Quality Level
분석
≥98% (TLC)
양식
powder
기술
thin layer chromatography (TLC): suitable
불순물
<10% water (Karl Fischer)
색상
white to light yellow
solubility
water: 50 mg/mL, clear, colorless
저장 온도
−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
애플리케이션
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).
기타 정보
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
신호어
Warning
유해 및 위험 성명서
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
표적 기관
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
개인 보호 장비
dust mask type N95 (US), Eyeshields, Gloves
가장 최신 버전 중 하나를 선택하세요:
이미 열람한 고객
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
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
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