Glycosylation is a very intriguing post-transductional modification of the proteins which sometimes seems to be critical for their antigenicity. Glycans appear to lack a discrete, folded structure; they are assembled without a template through a series of individually catalysed reactions. This arrangement can be particularly effective when glycans are used as tags to direct glycoprotein trafficking, adhesion events or other processes. In some cases, the role of a particular glycan is only evident in the context of a specific glycoconjugate. Therefore, obtaining a consistent glycoform profile in production is desired due to narrow concerns because a molecule can be defined by its carbohydrate structures. Glycosylation optimization will improve therapeutic and diagnostic efficacy and is an in progress goal for researchers in academia and industry alike.