The importance of Fc glycosylation of monoclonal antibodies (mAbs) with regard to biological activity is widely discussed and has been investigated in numerous studies. It is known that different glycan species contribute differently to the biological activity of therapeutic proteins.1 However, even if a certain glycan variant is known to have a positive impact on biological activity, it might not be easy to consistently produce such a glycosylation pattern. Cell line engineering or bioprocess optimization can enable increased glycosylation homogeneity or at least partially achieve a certain glycan pattern. However, these activities are timeconsuming and might compromise other key parameters, such as antibody yield. In addition, it is not economical to produce mAbs with a certain glycan pattern in analytical amounts using such tedious approaches.