Glycosylation

The process of glycosylation adds and removes sugar residues to and from oligosaccharides covalently linked to proteoglycans, glycoproteins, and glycosphingolipids. The functions of these oligosaccharides vary as widely as the proteins and lipids modified with them, and include tertiary structure stabilization, ligand-receptor binding, and correct subcellular localization. Generating and altering mature N-linked and O-linked glycans essential for proteoglycan and glycoprotein function requires glycosyltransferase and glycosidase activity for de novo oligosaccharide synthesis and remodeling. The resulting range of oligosaccharides is complex, and includes many functionally and structurally important sugar residues such as galactose, glucose, mannose, N-acetylgalactosamine, N-acetylglucosamine, fucose, and sialic acid. Increased proteoglycan, glycoprotein, and glycosphingolipid expression during cell differentiation or proliferation induces glycosyltransferase and glycosidase transcription. Given the essential nature of glycosylation, defects in this process most often present as inherited congenital developmental disorders including lysosomal storage diseases, such as Gaucher's and Fabry disease.

QIAGEN provides a broad range of assay technologies for glycosylation research that enables analysis of gene expression and regulation, epigenetic modification, genotyping, and signal transduction pathway activation. Solutions optimized for glycosylation studies include PCR array, miRNA, siRNA, mutation analysis, pathway reporter, chromatin IP, DNA methylation, and protein expression products.