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N-[(2R,4aR,6S,7R,8R,8aS)-8-Hydroxy-6-methoxy-2-(4-methoxy-phenyl)-hexahydro-pyrano[3,2-d][1,3]dioxin-7-yl]-acetamide is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

136983-79-4

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136983-79-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 136983-79-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,6,9,8 and 3 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 136983-79:
(8*1)+(7*3)+(6*6)+(5*9)+(4*8)+(3*3)+(2*7)+(1*9)=174
174 % 10 = 4
So 136983-79-4 is a valid CAS Registry Number.

136983-79-4Relevant academic research and scientific papers

Synthesis and characterization of pH responsive D-glucosamine based molecular gelators

Goyal, Navneet,Mangunuru, Hari P.R.,Parikh, Bargav,Shrestha, Sonu,Wang, Guijun

, p. 3111 - 3121 (2014)

Small molecular gelators are a class of compounds with potential applications for soft biomaterials. Low molecular weight hydrogelators are especially useful for exploring biomedical applications. Previously, we found that 4,6-O-benzylidene acetal protect

Probing the Acceptor Specificity of β-1,4-Galactosyltransferase for the Development of Enzymatic Synthesis of Novel Oligosaccharides

Wong, Chi-Huey,Ichikawa, Yoshitaka,Krach, Thomas,Narvor, Christine Gautheron-Le,Dumas, David P.,Look, Gary C.

, p. 8137 - 8145 (2007/10/02)

β-1,4-Galactosyltransferase has been investigated with regard to its acceptor specificity and used in the synthesis of galactosides with 5-thioglucose, glucal, deoxynojirimycin, modified N-acetylglucosamine, and glucose derivatives as acceptors. The galactoside products are potentially useful as endoglycosidase or glycosyltransferase inhibitors or as intermediates for the synthesis of complex oligosaccharides. The conformation of each enzyme product has been investigated with NMR; all arc shown to possess similar glycosidic torsional angles based on a significant NOE between H-1 of Gal and H-4 of the acceptor. Comparison of the transferase reactions with the β-1,4-galactosidase-catalyzed galactosyl transfer reactions indicates that the transferase reactions provide exclusively a β-1,4-glycosidic linkage while the galactosidase reactions predominantly form a β-1,6-glycosidic linkage.

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