When deciding on an antibody production strategy, researchers can choose between polyclonal or monoclonal antibodies. Both are used in a variety of research applications but have their own unique advantages and disadvantages.
Polyclonal antibodies (pAbs)
pAbs are produced by different B lymphocytes and recognize different epitopes of a single antigen. They can be generated in large quantities and rapidly (within several months of initiating immunizations), and at a lower cost than monoclonal antibodies (mAbs). Because they are heterogenous, any structural changes on one epitope are unlikely to significantly effect binding, and pAbs are more stable over a broad pH and salt concentration.
However, pAbs are at a disadvantage in avidity, since batch-to-batch variability will occur from production in different animals at different times. The quantity of pAbs obtained is also limited by the lifespan and size of the animal used. Furthermore, cross-reactivity may occur as pAbs recognize multiple epitopes.
Monoclonal antibodies (mAbs)
mAbs are produced by identical B lymphocytes which are clones of a single parent cell. Due to their homogeneity, they have high specificity and affinity. They are particularly useful in analyzing changes in molecular conformation, protein-protein interactions, phosphorylation states, and identifying single members of protein families. In addition, a key advantage mAbs have is their ability to be produced as a constant and renewable resource once the desired hybridoma has been generated.
On the other hand, mAb production can take up to a year or longer to develop the hybridized clone, so costs and times are higher than pAbs. Additionally, any changes in epitope structure or mAb labelling will negatively affect mAb binding ability.1
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Lipman, N. S., Jackson, L. R., & Trudel, L. J. (2005). Monoclonal Versus Polyclonal Antibodies: Distinguishing Characteristics, Applications, and Information Resources. ILAR Journal, 46(3), 258-268. https://doi.org/10.1093/ilar.46.3.258
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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