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
The therapeutic efficacy of antibodies is closely related to their ability to recognize and bind specific epitopes on target antigens. Epitopes, or antigenic determinants, are a group of amino acids or other chemical groups that are part of a molecule to which an antibody attaches itself. Epitope characterization can help reveal the mechanism of antibody binding and apply intellectual property (patent) protection for novel antibodies, in addition to designing antibodies with high specificity and minimal cross-reactivity.
Understanding the differences between antibody specificity and selectivity is essential for designing and interpreting antibody-based assays in research for experimental accuracy and data interpretation. Antibody specificity refers to an antibody's ability to recognize and bind to a particular epitope—a unique part of an antigen that elicits an immune response.
Antibody-based assays are essential tools in biomedical research, providing the means to detect, quantify, and visualize specific proteins or antigens within complex biological samples. These assays' efficacy hinges on the antibodies' precise properties. While affinity, avidity, specificity, and selectivity are fundamental to antibody performance, the ultimate impact of these properties is heavily influenced by the experimental context in which the antibody is employed.
Biologics, particularly antibodies, have become indispensable in biomedical research and therapeutic development. Research-use-only (RUO) biologics play a pivotal role in preclinical studies, providing researchers with the necessary tools to explore antibody functions and therapeutic potential in vivo.
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