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
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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