Monoclonal Antibody Scholarly
The
immune system in vertebrates is continuously evolving to protect itself from different intruding pathogens. The immune responses rotate around some innate mechanisms, including adaptive processes such as producing antibody (Ab)
molecules that can bind to all molecular structures of the
microbial pathogen (bacteria, viruses, fungi, nematodes, and other parasites) and can keep pace with the diversified
mutations in anorganism. An antigen is defined as a molecule or part of a molecule that can be recognized by the
immune system as a foreign entity. The challenge of the
immune system is thus combated in two ways. First, through an antibody diversity mechanism, B lymphocytes produce varied antibodies specific for a new antigen (epitope) expressed by a pathogen by shuffling and reshuffling its genetic constituents. Second, paratope-encoding genes of the antibody are mutated rapidly to cope and bind strongly with the
epitope of the antigen. Thus, these generated antibodies are better at binding with the antigen with greater affinity and high specificity.
Therefore, antibodies are useful research tools in diagnosis and therapy, as they can recognize and bind specifically and strongly with respective antigens. Polyclonal antibodies mixtures contain different antibodies developed in the blood of immunized animals from different cell types. As most antigens bear multiple epitopes, they can stimulate the proliferation and differentiation of a variety of B-cell clones. Thus a heterogeneous pool of serum antibodies can be produced with specificity for particular epitope(s) of the antigen.
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