How are primary antibodies made?
At their origins, all primary antibodies are made from building blocks from immunesystems of the hosts. These building blocks are called complementarity-determining regions (CDRs). CDR is a complex topic which we will not go into in this article so for more information on CDRs you can visit this Wikipedia page.
Traditionally, scientists made polyclonal primary antibodies by immunizing the host animals, typically rabbit, goat, chicken, mice and variety of mammalian and avian species, with antigens, inciting the immune responses which produce antibodies, and extracting (by a method called immune-affinity purification chromatography) the resulting antibodies from the host’s sera or eggs.
In 1975, Georges Köhler and César Milstein developed the monoclonal antibody technology. In 1985, George P Smith developed the method called phage-display, which marks the start of the antibody engineering era where antibody development moves from hijacking hosts’ adaptive immune systems towards rational design.
However the majority of antibodies used today, in the 2020s, are still made from host animals at some point in its production. A truly animal free primary antibody development solution has yet to be invented, primarily because scientists have not found an animal-free mechanism that can replace the somatic maturation of B-cells. Without such mechanism, it is impossible to achieve the same level of affinity and specificity of naturally matured antibodies. This opinion is from the author of this article and is up for debate, if you believe otherwise you can send your arguments to [email
protected] or post on our Facebook page.