Glycans are one of the major types of macromolecules in the cell that play essential roles in various biological processes. Compared with proteins and nucleic acids, analyzing glycans in situ is more challenging. Glycans are not primary gene products, and their genetically encoded tags cannot be used for tracking. Lectins and antibodies are essential tools for glycan labeling but can suffer from limitations relating to specificity and affinity.

Azide- and alkyne-modified monosaccharides are highly specific tools for studying glycoproteins and post-translational protein modification through metabolic labeling in vivo. These unnatural sugars are cell-permeant and can be metabolized by cellular glycosyltransferases to incorporate instead of their natural monosaccharide counterpart on the glycan chain both intracellularly and on the cell surface. The subsequent chemoselective click reaction allows the labeled glycan to be tagged with a fluorophore and visualized and tracked in cells, tissues, and living organisms.

We offer azide- and alkyne-modified analogs of N-acetylmannosamine, N-acetylglucosamine, and N-acetylgalactosamine for proteomic analysis of post-translational modifications and identifying glycoprotein fingerprints associated with cell differentiation and malignant transformation.