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3-(2,3,4,6-tetra-O-benzyl-α-D-galactopyranosyl)propanoic acid is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

213972-49-7

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213972-49-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 213972-49-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,1,3,9,7 and 2 respectively; the second part has 2 digits, 4 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 213972-49:
(8*2)+(7*1)+(6*3)+(5*9)+(4*7)+(3*2)+(2*4)+(1*9)=137
137 % 10 = 7
So 213972-49-7 is a valid CAS Registry Number.

213972-49-7Relevant academic research and scientific papers

Sweet and salted: Sugars meet hydroxyapatite

Sandri, Monica,Natalello, Antonino,Bini, Davide,Gabrielli, Luca,Cipolla, Laura,Nicotra, Francesco

supporting information; experimental part, p. 1845 - 1848 (2011/10/01)

Carbonated hydroxyapatite (CHA) has been successfully biodecorated with carbohydrate derivatives, via silylation of the hydroxy groups of the apatite and subsequent covalent bonding with a suitably functionalized carbohydrate moiety. The presented procedu

Facile preparation of an orthogonally protected, pH-sensitive, bioconjugate linker for therapeutic applications

Fletcher, Steven,Jorgensen, Michael R.,Miller, Andrew D.

, p. 4245 - 4248 (2007/10/03)

(Chemical Equation Presented) We describe the facile, three-step synthesis of an orthogonally protected, pH-sensitive linker (8), based on maleic acid, and report its application to the preparation of a pH-sensitive phospholipid (20) for potential use in drug and gene delivery. In addition, we highlight the benefits of our linker over the use of the commercially available cis-aconitic anhydride (4).

Differential carbohydrate recognition of two GlcNAc-6-sulfotransferases with possible roles in L-selectin ligand biosynthesis

Cook, Brian N.,Bhakta, Sunil,Biegel, Teresa,Bowman, Rendra G.,Armstrong, Joshua I.,Hemmerich, Stefan,Bertozzi, Carolyn R.

, p. 8612 - 8622 (2007/10/03)

Two human GlcNAc-6-sulfotransferases, CHST2 and HEC-GlcNAc6ST, have been recently identified as possible contributors to the inflammatory response by virtue of their participation in L-selectin ligand biosynthesis. Selective inhibitors would facilitate their functional elucidation and might provide leads for antiinflammatory therapy. Here we investigate the critical elements of a disaccharide substrate that are required for recognition by CHST2 and HEC-GlcNAc6ST. A panel of disaccharide analogues, bearing modifications to the pyranose rings and aglycon substituents, were synthesized and screened for substrate activity with each enzyme. Both GlcNAc-6-sulfotransferases required the 2-N-acetamido and 4-hydroxyl groups of a terminal GlcNAc residue for conversion to product. Both enzymes tolerated modifications to the reducing terminal pyranose. Key differences in recognition of an amide group in the aglycon substituent were observed, providing the basis for future glycomimetic inhibitor design.

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