Ensuring antibody stability is crucial during antibody generation and utilization, as instability can lead to reduced yields, lower efficacy, harmful immune reactions, patient-associated complications, and limited or lost function when working in extreme conditions or during long-term storage.
The main factors affecting stability are the antibody’s format, structure, state of aggregation, and susceptibility to proteases. There are several methods to monitor the retention of biological function, including ELISA, Western blotting and affinity analysis (e.g. SPR/Biacore), during and after production. Additionally, circular dichroism, nuclear magnetic resonance, and mass spectroscopy have been used to indicate stability in the past.1
To overcome these issues with stability, one should strive to:
Eliminate or minimize proteolysis, fragmentation or aggregation during antibody production.
Stabilize the antibody format at the molecular level through sequence or domain swapping, CDR grafting, insertion of additional disulfide(s), or other chemical modifications.
Ensure the use of appropriate buffers, additives and excipients.
Carefully consider storage conditions including container, temperature, and moisture.
Stability directly impacts an antibody’s efficacy, safety, and shelf life, making it a critical aspect of biologics development. At Biointron, we are dedicated to accelerating antibody discovery, optimization, and production. Our team of experts can provide customized solutions that meet your specific research needs. Contact us to learn more about our services and how we can help accelerate your research and drug development projects.
Ma, H., Ó’Fágáin, C., & O’Kennedy, R. (2020). Antibody stability: A key to performance - Analysis, influences and improvement. Biochimie, 177, 213-225. https://doi.org/10.1016/j.biochi.2020.08.019
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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