Glycoamino Acids

The side chains of amino acid residues of proteins and peptides are frequently modified with glycans which play crucial roles in a variety of cellular activities such as cell growth, differentiation, transformation, and adhesion. These glycans are covalently attached to the amino acid in a co- or post-translational process. The most common forms of protein glycosylation are N-linked and O-linked glycans. For O-linked glycans, an N-acetylgalactosamine residue is alpha-linked to the side chain oxygen of either a serine (Ser) or threonine (Thr). The mucins are an example of glycoproteins that are heavily O-glycosylated. N-linked glycans are attached to the glycoprotein via attachment of an N-acetylglucosamine linked to an asparagine residue (Asn). Glycosylation occurs less commonly on other amino acid residues such as tyrosine, and tryptophan for example. Both N- and O-linked glycans can be extended to different common core structures which can be further elaborated with different terminal glycan structures. Glycosylated amino acid are valuable reagents for the synthesis of glycopeptides and as standards to study the properties of these important biomolecules.

We have provided researchers with the most extensive selection of commercially available, high purity glycosylated amino acids (glycoamino acids) for over 25 years.