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Protein glycosylation is a complex posttranslational modification that manipulates the biological activity and function of therapeutic glycoproteins. Glycan composition has been the target of modification to enhance the safety and efficacy of glycoprotein therapeutics. Glycans are the most complex and heterogeneous class of molecules due to their non-template-driven biosynthetic process, consequently making glycan characterization difficult. It is essential to apply several orthogonal methods to measure individual parameters such as glycosylation site analysis, oligosaccharide sequence, and monosaccharide content of a therapeutic glycoprotein. The importance of studying aberrant glycosylation in cancer is highlighted by the case of the prostate specific antigen (PSA). PSA is a clinical biomarker for prostate cancer, a disease estimated to have led to 375[thin space (1/6-em)]000 deaths and 1.4 million new cases worldwide in 2020.