PhyTip® Normal Phase Columns for Enrichment of Glycans

Among the co-translational and post-translational modifications, the cellular process of enzymatic addition of carbohydrates to proteins, called glycosylation, has been a subject of much attention. The resulting glycoprotein is modified with branched or unbranched chains of carbohydrates that form oligosaccharides and polysaccharides, which are simply called glycans. The addition of glycans can occur at asparagine residues, called N-linked, or at the hydroxal oxygens of serine and theronine residues, called O-linked. Glycoproteins are an important subclass of proteins and are involved in a diverse set of cellular functions including signal transduction, inflammation, cell-cell interactions, and development.  There is a high recent interest in the biopharmaceutical industry towards glycoproteins. Glycoproteins are among the high potential targets because of their crucial function in cellular processes. In addition to the interest in this class of proteins as drug targets, researchers are conscious of the fact that glycans are implicated in activity and efficacy of therapeutic peptides and proteins. Any biotherapeutic drug development program takes glycosylation into serious consideration as a means of producing a better product with higher production reproducibility.