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Monoclonal antibodies are one of the most successful reagents for a wide range of applications. Their specificity, ease of production and conjugation, and general low toxicity make them advantageous in comparison to small molecules. Check our frequently asked questions (FAQs) page about monoclonal antibodies for a complete overview of all steps of this robust process for antibody generation.
Monoclonal antibodies are one of the most successful biologics in use for a variety of applications. The benefits of using these molecules typically stem from their strong selectivity, specificity, and binding affinity.
Moreover, most monoclonal antibodies are currently well-characterized (sequence, affinity, etc.) and can be easily produced in recombinant systems such as Chinese hamster ovary (CHO) and Human embryonic kidney (HEK) cell lines. The production of these reagents in well-defined systems and media ensures a robust batch-to-batch reproducibility and high purity, essential for many applications.
Given the selectivity and specificity of these molecules, monoclonal antibodies can be tailored to recognize and differentiate between similar antigens or epitopes, including the ones containing SNPs (single nucleotide polymorphisms) or harboring specific post-translational modifications. For this reason, monoclonal antibodies are highly sought molecules for differential diagnostics of complex diseases.
In many cases, antibody-based diagnostics ensure the determination of disease severity or disease types in the early stages of development, helping clinicians improve survival by matching the best treatment options with specific patients.
Antibodies are also very stable and, thus, adaptable to different test formats. Nowadays, these molecules are essential both in clinical diagnostics and surveillance studies. In these tests, antibodies are mostly used in conjugation with enzymatic (colorimetric) or fluorescent tags for techniques like ELISA (enzyme-linked immunosorbent assay) or flow cytometry.
In both cases, antibody validation in the target application and sample type is a decisive factor for test accuracy and precision. This influence stems from the nature of the tags and test support (immobilized like ELISA applications or in suspension like in flow cytometry) that can change antibody conformation and affinity; and sample pre-treatment that can modify how antigens are exposed or displayed within the sample.
Monoclonal antibodies are one of the most successful biotherapeutic drugs used in the treatment of many types of cancer and autoimmune conditions. Their enhanced safety and lower toxicity in comparison to chemotherapy drugs are proven to reduce adverse side-effects and improve patient survival and well-being.
The success of monoclonal therapies in these complex disease landscapes can also be explained by their intrinsic properties. Antibodies consist of two identical antigen-binding regions (Fab) and a single conserved region known as Fc (fragment crystallizable region). While the former is responsible for blocking specific protein interactions, the latter can modulate the immune response of patients by engaging specific immune cells or stimulating the production of specific signals that can either enhance or suppress the immune response.
These modulating properties of the Fc region depend on the nature, abundance, and distribution of glycans on its surface. For this reason, these responses can be further fine-tuned by glycoengineering the Fc region of these molecules, a process that is now recurrently performed to develop novel immunotherapies.
Monoclonal antibody therapy can also benefit the treatment of certain infectious diseases. In comparison to antibiotics which are unable to discriminate between beneficial and infectious bacteria, antibodies can be designed to target specific disease markers on the surface of pathogens. This specificity ensures that the natural balance of the microbiome is unaffected, further decreasing the risk of subsequent infection recurrence.
Moreover, antibodies may be the only suitable option in the treatment of viral diseases that cannot be prevented by vaccination such as HIV or hepatitis C. In these instances, antibodies can act as neutralizing agents (by blocking cell-virus interactions) and/or promote the clearance of viral particles from the patient’s system.
Monoclonal antibodies are prized for their selectivity, specificity, and binding affinity. These properties in conjugation with their ease of production in recombinant mammalian systems make them successful in a wide array of applications.
In diagnostics, antibodies can be easily conjugated with enzymatic or fluorescent tags and used for fast screening in ELISA or flow cytometry platforms, among others. In therapy, antibodies are favored due to their low toxicity and specificity, which makes them beneficial for the treatment of cancer and autoimmune diseases.
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