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130177-78-5

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130177-78-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 130177-78-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,0,1,7 and 7 respectively; the second part has 2 digits, 7 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 130177-78:
(8*1)+(7*3)+(6*0)+(5*1)+(4*7)+(3*7)+(2*7)+(1*8)=105
105 % 10 = 5
So 130177-78-5 is a valid CAS Registry Number.

130177-78-5Downstream Products

130177-78-5Relevant articles and documents

Automated Solution-Phase Synthesis of S-Glycosides for the Production of Oligomannopyranoside Derivatives

Kern, Mallory K.,Pohl, Nicola L. B.

, (2020/06/08)

Thioglycosides are more resistant to enzymatic hydrolysis than their O-linked counterparts, thereby becoming attractive targets for carbohydrate-based therapeutic development. We report the first development of methods for the site-selective incorporation

Intramolecular aglycon delivery for (1 → 2)-β-mannosylation: Towards the synthesis of phospholipomannan of Candida albicans

Gannedi, Veeranjaneyulu,Ali, Asif,Singh, Parvinder Pal,Vishwakarma, Ram A.

supporting information, p. 2945 - 2947 (2014/05/06)

A high yielding method for 1,2-cis-β-D-mannosylation by intra-molecular aglycon delivery (IAD) through p-methoxy benzyl ether/acetal exchange and phenylsulfoxide donor is reported, along with its application in iterative assembly of antigenic (1 → 2)-β-pe

'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks

Barry, Conor S.,Cocinero, Emilio J.,Carcabal, Pierre,Gamblin, David P.,Stanca-Kaposta, E. Cristina,Remmert, Sarah M.,Fernandez-Alonso, Maria C.,Rudic, Svemir,Simons, John P.,Davis, Benjamin G.

supporting information, p. 16895 - 16903 (2013/12/04)

N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit -Man3GlcNAc2- lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an indispensable role, associated perhaps with its structure, its unbiased conformation and the potential modulating role of solvation are unknown; both have now been explored through a combination of synthesis, laser spectroscopy, and computation. The proximal -GlcNAc-GlcNAc- unit acts as a rigid rod, while the central, and unusual, -Man-β-1,4-GlcNAc- linkage is more flexible and is modulated by the distal Man-α-1,3- and Man-α-1,6- branching units. Solvation stiffens the 'rod' but leaves the distal residues flexible, through a β-Man pivot, ensuring anchored projection from the protein shell while allowing flexible interaction of the distal portion of N-glycosylation with bulk water and biomolecular assemblies.

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