Abstract
Monoclonal antibodies (mAbs) have emerged as a therapeutic tool to treat several diseases, including cancer. mAbs accelerate cellular and humoral response to block signals, receptors, or immune checkpoints via drug target therapy or immunotherapy. Generation of human antibodies in animals (mouse or rabbit) from polyclonal to mAbs and from murine to chimeric antibody and further modify to fully humanized mAbs has become an attractive therapeutic tool for clinical studies and academic research. Posttranslational modifications, half-life, and immunogenicity can affect the mAb efficacy and avidity. However, antibody production and purification are challenging tasks. Protein A/G affinity purification has been used to purify mAbs from hybridoma culture or transiently expressed in cell culture. Specific binding of mAbs to its antigen happens as it binds to its single epitope. In this chapter, we discuss the transient expression and purification of mAbs in mammalian cells.
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