Phage display technology is a powerful technique for antibody discovery. It is often used to identify high-affinity interactions between antibody fragments (e.g. VHHs) and target proteins for the production of monoclonal antibodies. Originally developed in the mid-1980s, phage display is a key technology for antibody engineering, drug discovery, protein-protein interactions, and vaccine development.1
By genetically engineering the bacteriophage's coat protein, the VHH (heavy-domain camelid antibody fragment) sequence can be linked to the phage DNA, enabling the displayed antibody fragment to be encoded by the viral genome. This facilitates the production of a diverse library of phage particles, each carrying a different antibody fragment on its surface.
These phage display libraries screen the phage particles to identify antibodies that bind to specific target antigens in a process called panning, which involves repeated rounds of binding, washing, elution, and amplification. Once identified, these antibodies can be further optimized for improved affinity, specificity, and therapeutic properties. Additionally, phage display has facilitated the discovery of small peptide-based drugs and the identification of potential drug targets.
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.
Hammers, C. M., & Stanley, J. R. (2014). Antibody Phage Display: Technique and Applications. The Journal of Investigative Dermatology, 134(2), e17. https://doi.org/10.1038/jid.2013.521
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.
ScientistとScience Exchangeとのご利用可能です。
