Does antibody generation raise a number of questions like what is the difference between their classes, forms, and types? And how do recombinant monoclonal antibodies (rAbs) overcome the drawbacks of classical monoclonal antibodies (mAbs)?
Monoclonal antibodies are ubiquitous in biomedical research and medicine. They are used to fight, diagnose, and study disease, and to develop and test new drugs. Antibodies are divided into some classes or isotypes, several subtypes, and forms, and can be generated in vivo or in vitro.
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Antibodies (Abs) are blood glycoproteins that belong to the immunoglobulin superfamily and make up the majority of the gamma globulin fraction of blood proteins. However, they can also be found in other body fluids.
They are secreted by B cells or membrane-bound B cells through their Fc region to the B cell receptor (BCR) in response to foreign organisms or the presence of antigens (bacteria, viruses, etc.). Each antibody contains a variable region of Fab which has a paratope at the end that is specific for a particular antigenic epitope.
When these two structures bind together, Ab can tag foreign bodies or infected cells to neutralize them directly or allow other cells of the immune system to attack them. Stomach production is a major function of the humoral immune system.