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  • importx posted an update 1 month, 2 weeks ago

    In general, polyclonal antibodies are made by collecting blood from an immunized animal stimulated with a target antigen, which can be provided all the time as long as the animal is still alive, while monoclonal antibodies are produced continuously by immunizing the host animal with the target protein and then extracting B cells that recognize and respond to the antigen and fuse them with myeloma cells to become permanent culturable cells, widely used in laboratory research, diagnostic products, and immunotherapy.

    Compared to polyclonal antibodies, monoclonal antibodies have multiple advantages, featured by strong specificity for a single epitope, little or no variability, and the easy operation to modify and customize in terms of different needs, thereby turning out to be the most suitable candidate for recombinant antibodies (rAbs). The rAbs are obtained through sequencing of the animal’s immune cells and inserting the gene into a suitable cell strain, such as bacterium, yeast, and mammalian cells. Even if the original cell strain dies or is mutated, the desired cell strain can be generated by gene insertion since the antibody is definitive.

    The recombinant antibody production firstly requires the high-quality construction of production cell line. Current expression levels of engineering cell lines used for recombinant antibody production internationally can reach 20-70pcd and a variety of animal cells have been applied into the antibody production according to their distinct characteristics. In recent years, the development of engineering cell lines mainly focused on cell engineering techniques that improve the growth and expression ability of the host, site-directed integration techniques that overcome the position effects during the random vector integration, and flow cytometry and high-throughput screening that enhance the screening throughput and efficiency of recombinant cells.

    The complex antibody structure of tetrameric glycoprotein and the multi-step extracellular expression both pose a potential challenge to a perfect antibody production process. Only after translation, folding, assembly and glycosylation of both light and heavy chains, can the antibody be equipped with biological activity. It has been proved that the post-translational modification of recombinant antibodies by host cells directly affects the clinical efficacy and immunogenicity of antibody drugs.

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