We offer a series of chondroitin sulphates (CS) and dermatan sulphates (DS) that cover the principal isomers found in mammalian tissues. Thus in addition to the common CS-A (GlcA – GalNAc,4S), CS-C (GlcA – GalNAc,6S) and DS (IdoA – GalNAc,4S; also called CS-B), we supply CS and DS with variable contents of diCS-E and diDS-E disaccharides (GlcA – GalNAc 4S, 6S and IdoA – GalNAc, 4S,6S respectively). Preparation of CS-E and DS-E was carried out by addition of 6-O-sulphate groups to CS-A and DS using specific chemical methods to synthesise the 4,6-di-O-sulphated GalNAc residue. The identity of the products was determined by 1H NMR and disaccharide analysis. We also supply CS-D which contains the disulphated diD-isomer GlcA,2S – GalNAc,6S
Mizumoto, S., Yamada, S. & Sugahara, K. (2015) Molecular interactions between chondroitin–dermatan sulfate and growth factors/receptors/matrix proteins. (2105) Current Opinion in Structural Biology. 34, 35-42
Derbal, I., Lortat-Jacob, H. & Kwok, J. (2017) Chondroitin sulfates and their binding molecules in the central nervous system. Glycoconjugate J. 34, 363 - 376
Research in cell growth and development protein binding studies.
Chondroitin Sulphate (CS) and Dermatan Sulphate (DS) are common constituents of the pericellular environment of most mammalian organs and tissues. They are well-known as structural elements of the ECM but over the past 10 years or so peer-reviewed papers have revealed their importance in cell growth and differentiation, particularly in the embryonic nervous system. The effects of CS and DS on cell development are dependent on interactions with peptide growth factors and morphogenic proteins. These interactions often require specific molecular characteristics of the CS and DS chains in which relatively rare disulphated disaccharides (diCS-E and/or diDS-E units) are key components. To aid research in this field we offer a series of CS and DS polymers that cover the principal isomers found in mammalian tissues. These products also have application in protein binding studies or competitive processes, especially involving comparisons between the effects of different levels and patterns of sulphation on the specificity of interactions and influences on protein conformation and activity.
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