The conjugation of carbohydrate moieties, or saccharides, onto various glycosyl acceptors, be it a protein, lipid, or any organic molecule, defines glycosylation. It is a very prevalent posttranslational nontemplated modification. Glycosylation is highly modular; carbohydrate building blocks are repeatedly linked and assembled in varying lengths, branches, and configurations. Being nontemplated, glycosylation does not have canonical patterns, which can result in high diversity and an extensive repertoire of biologically functional molecules.Despite their seemingly nontemplated assembly, glycans synthesis does appear to adhere to some common structural patterns. Humans use nine monosaccharides in various glycoconjugate forms (Table 1).Glycan residues are conjugated on asparagine (N-glycan) or serine/ threonine (O-glycans) residues (Figure 1) to form glycoproteins. Two N-acetylglucosamine (GlcNAc) and three mannose residues often serves as the core of N-glycans, which are often highly branched.Conversely, O-glycans are linked with N-acetylgalactosamine (GalNAc) moiety and are often less branched than N-glycans. Although N-glycan attachment to proteins occurs on asparagines (N) within the consensus (N glycan sequon) NXS/T, where X is any amino acid except proline, there is no predictive sequon for O-glycans. Rather, O-glycans often occur in "bottle brush" conformations in variable