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Therapeutic proteins are a key concentrate in a lot of pharmaceutical portfolios on account of their efficient treatment of a wide spectrum of illnesses such as cancers and immune disorders [1]. Fusion proteins have been engineered to optimize the pharmacokinetic and pharmacodynamic properties with the active protein and to boost Fc domain effector functions or boost the serum half-life [2, 3]. Glycotherapeutics include monoclonal antibodies and recombinant fusion proteins [4]. The latter have received a great deal focus because the getting that fusing biologically Joseph Zaia [email protected] of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA 02118, USA Analytical Development, Pharmaceutical Sciences, Takeda Improvement Center Americas, Inc., Lexington, MA 02421, USAactive proteins together with the fragment of human-derived Ig (such as IgG, IgA, IgD, IgM, and IgE) can drastically in.