nlinked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human igg we studied the variations in nlinked glycosylation of human igg molecules derived from 105 different stable cell lines each expressing one of the six different antibodies antibody expression was based on glutamine synthetase selection technology in suspension growing chok1sv cells the glycans detected on the fc fragment were mainly of the corefucosylated complex type containing zero or one galactose and little to no sialic acid the glycosylation was highly consistent for the same cell line when grown multiple times indicating the robustness of the production and glycan analysis procedure however a twofold to threefold difference was observed in the level of galactosylation andor noncorefucosylation between the 105 different cell lines suggesting clonetoclone variation these differences may change the fcmediated effector functions by such antibodies large variation was also observed in the oligomannose5 glycan content which when present may lead to undesired rapid clearance of the antibody in vivo statistically significant differences were noticed between the various glycan parameters for the six different antibodies indicating that the variable domains andor light chain isotype influence fc glycosylation the glycosylation altered when batch production in shaker was changed to fedbatch production in bioreactor but was consistent again when the process was scaled from 400 to 5000 l taken together the observed clonetoclone glycosylation variation but batchtobatch consistency provides a rationale for selection of optimal production cell lines for largescale manufacturing of biopharmaceutical human igg