Demonstrating Comparability of Antibody Glycosylation during Biomanufacturing

@inproceedings{2005DemonstratingCO,
  title={Demonstrating Comparability of Antibody Glycosylation during Biomanufacturing},
  author={},
  year={2005}
}
  • Published 2005
Therapeutic antibodies of the IgG class produced in mammalian expression systems bear two N-glycans in the CH2 domain of the Fc region. This glycosylation is highly heterogeneous and rMAbs produced in CHO, NSO and other popular cell systems typically contain up to 30 or so different types of glycans at each of the two Fc N-glycosylation sites. This ‘microheterogeneity’, together with the combinatorial pairing of glycans on the IgG heavy chains, leads to the presence of large numbers of… CONTINUE READING

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