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5-ethylamino-2,4-dinitrophenyl 2,3,4,6-tetra-O-acetyl-1-thio-β-D-galactopyranoside is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

857631-72-2

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857631-72-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 857631-72-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,5,7,6,3 and 1 respectively; the second part has 2 digits, 7 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 857631-72:
(8*8)+(7*5)+(6*7)+(5*6)+(4*3)+(3*1)+(2*7)+(1*2)=202
202 % 10 = 2
So 857631-72-2 is a valid CAS Registry Number.

857631-72-2Relevant academic research and scientific papers

Synthesis of a phenyl thio-ss-D-galactopyranoside library from 1,5-difluoro-2,4-dinitrobenzene: Discovery of efficient and selective monosaccharide inhibitors of galectin-7

Cumpstey, Ian,Carlsson, Susanne,Leffler, Hakon,Nilsson, Ulf J.

, p. 1922 - 1932 (2007/10/03)

The galectins are a family of β-galactoside-binding proteins that have been implicated in cancer and inflammation processes. Herein, we report the synthesis of a library of 28 compounds that was tested for binding to galectins-1, -3, -7, -8N and -9N. An aromatic nucleophilic substitution reaction between 1,5-difluoro-2,4-dinitrobenzene and a galacto thiol gave 5-fluoro-2,4-dinitrophenyl 2,3,4,6-tetra-O-acetyl-l-thio-β-D- galactopyranoside. This versatile intermediate was then modified in a two dimensional manner: either by further substitution of the second fluoride by amines or thiols, or by reduction of the nitro groups and acylation of the resulting amines, or both. Deacetylation then gave a library of aromatic β-galactosides that showed variable inhibitory activity against the different galectins, as shown by screening with a fluorescence-polarisation assay. Particularly efficient inhibitors were found against galectin-7, while less impressive enhancements of inhibitor affinity over methyl β-D-galactopyranoside were found for galectin-1, -3, -8N and -9N. The best inhibitors against galectin-7 showed significantly higher affinity (K d as low as 140 μM) than both β-methyl galactoside (K d 4.8 mM) and the unsubstituted β-phenyl thiogalactoside (non-inhibitory). The best inhibitors against galectin-7 were poor against the other galectins and thus have potential as structurally simple and selective tools for dissecting biological functions of galectin-7. The Royal Society of Chemistry 2005.

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