Abstract: Glycosylation is a process that involves the addition of sugar moieties or glycans to different types of molecules, including proteins, lipids, and nucleic acids. Among these, protein glycosylation is one of the most prevalent forms of post-translational modification, playing a crucial role in biological complexity. With more than ten monosaccharides identified within mammalian brain cells and more than 1 × 1012 possible combinations, the heterogeneity of glycosylation is extensive (Conroy et al., 2021). The diversity of glycans and the complexity of their structures allow for a wide range of protein functions. N-glycans are one of the most abundant forms of glycans and are involved in various cellular functions. N-glycans can be added to proteins at specific sequons, Asn-X-Ser/Thr, and are classified into three main types in mature glycoproteins: high mannose, complex, and hybrid. High mannose N-glycans consist of 5–9 mannose residues linked to a chitobiose core and undergo processing into complex or hybrid forms in the Golgi apparatus (Varki et al., 2017). Complex N-glycans are more diverse and contain various branched structures such as antennae with fucose, galactose, and sialic acid residues. Hybrid N-glycans contain one or more complex branches in conjunction with an oligomannose branch (Fisher and Ungar, 2016). Understanding the specific functions of these different types of N-glycans in protein regulation, folding, and function is an active area of research in the life sciences, including glycobiology.