Creative Biolabs provides excellent services for the construction and screening of immune antibody library generated by our advanced phage display technology. Our professional scientists can generate antibody libraries from diverse species, including common laboratory animals [e.g. rodents, rabbit, chicken, dog and monkey (NHP)], and some infrequent antibody sources such as human, camel, shark, bovine, alligator, and so on.
Over the past decades, phage display has been proven to be a powerful technology to 'display' millions or even billions of different peptides or proteins. It is now a common choice for the studies of protein-protein, protein-peptide and protein-DNA interactions. The technique is mainly based on the using of bacteriophages, such as T4, T7 and the most common M13 filamentous phage. By fusing a protein encoding gene with bacteriophage coat protein gene, the interested protein can be displayed on the phage surface, which can be then used to detect its interaction or binding ability with other molecules. One of the successful applications of phage display technology is the isolation of monoclonal antibodies using large capacity phage antibody libraries.
Currently, constructing and screening immune antibody library via phage display technology have become a major choice for the production of monoclonal antibody with high specificity and affinity. Compared with the conventional hybridoma technology, the generation of immune antibody libraries is not limited by the requirement of fusion partners, which expands the possibility to develop monoclonal antibodies from a much broader range of species. In general, the phage-displayed immune antibody libraries are constructed in scFv and Fab format, and the antibody gene repertoire is created from the immunoglobulin gene of either spleen B cells (for immunized animals) or peripheral blood B cells (for immunized donors). Theoretically, on the basis of appropriate genome information, phage display technology has potential to construct antibody libraries for every species and develop the corresponding monoclonal antibodies.
At Creative Biolabs, we have succeeded in generating monoclonal antibodies from various host species, including but not limited to:
Creative Biolabs has years of experience in the field of antibody development and phage display technology. Our scientists are confident in generating antibody libraries with a diversity of 108-10, which can meet the needs of the vast majority of research. Meanwhile, we also have extensive experience in designing the most appropriate biopanning strategy to select reliable antibodies with high specificity and affinity. In addition to the regular antibody libraries of experimental animals, our scientists are also able to generate a series of unique antibody libraries from other species, such as human, guinea pig, shark and alligator. As one of the well-recognized industry leaders, Creative Biolabs is committed to offering the most comprehensive antibody production services and providing the best service with high efficiency and quality.
Fig. 1 Isolation of rNIE specific monoclonal antibodies.1, 2
The research focuses on the isolation of monoclonal antibodies targeting Strongyloides stercoralis using an immune antibody phage display library derived from individuals infected with lymphatic filaria. The study's significance lies in demonstrating the broader applicability of immune antibody libraries, showing they can generate antibodies for related infections, not just the specific disease they were initially designed for. The results revealed successful isolation and characterization of multiple antibodies against S. stercoralis, with diverse gene usage and strong binding affinities. Immunized antibody libraries in this study provided a targeted yet diverse repertoire of antibodies that could be rapidly screened and applied to emerging infectious diseases, particularly those closely related to the immune library's original target, showcasing their potential in diagnostic and therapeutic applications for neglected tropical diseases.
Immunized antibody libraries are derived from B cells of individuals exposed to a specific antigen, resulting in a repertoire of antibodies with high affinity and specificity. These libraries are enriched for antigen-specific antibodies, allowing for the rapid isolation of monoclonal antibodies that are already optimized through natural immune processes, which often results in better binding characteristics and lower cross-reactivity compared to those derived from naïve libraries.
Immunized antibody libraries provide a diverse collection of high-affinity antibodies that have undergone affinity maturation in vivo. This process increases the likelihood of identifying potent therapeutic candidates with strong antigen specificity and minimal off-target effects. The antibodies derived from these libraries are particularly useful in developing treatments for infectious diseases, cancers, and autoimmune disorders.
Common types of immunized antibody libraries include those derived from humans, animals (such as mice, rabbits, or llamas), and even genetically engineered models. Each type of library has its own advantages, with human libraries offering the benefit of direct therapeutic application, while animal libraries can provide a broader range of antibody diversity and unique binding properties due to species-specific immune responses.
The selection process typically involves phage display technology, where the library is screened against a target antigen. Antibodies that bind to the antigen are enriched through multiple rounds of panning. These enriched clones are then expressed and further characterized for their binding affinity, specificity, and functional activity, leading to the identification of promising monoclonal antibodies.
Immunized antibody libraries are particularly effective in generating antibodies against difficult targets, such as conformational epitopes or rare antigens. The natural immune response, combined with the diversity of an immunized library, increases the chances of isolating antibodies that recognize challenging targets, making these libraries valuable tools in drug discovery and diagnostic development.
Affinity maturation is a critical process that occurs naturally during an immune response, where B cells produce antibodies with progressively higher affinity for the antigen. This process is reflected in immunized antibody libraries, where the antibodies have already undergone this optimization, resulting in a higher likelihood of isolating monoclonal antibodies with strong binding affinities and desired functional properties.
Immunized antibody libraries differ from synthetic libraries in that they are derived from an organism's natural immune response, leading to a more biologically relevant and diverse repertoire. While synthetic libraries are designed for broad applicability and can target a wide range of antigens, immunized libraries often yield higher affinity antibodies with greater specificity, especially for closely related or complex antigens.
One of the challenges is the potential for a limited diversity in the antibody repertoire, as it is skewed towards the immunizing antigen. Additionally, generating and maintaining immunized libraries can be resource-intensive. However, these challenges are often outweighed by the advantages of high-affinity, antigen-specific antibodies that can be rapidly isolated and optimized.
Monoclonal antibodies from immunized antibody libraries are highly effective in therapeutic applications, particularly in oncology, infectious diseases, and autoimmune disorders. They are also valuable in diagnostic assays, where high specificity and sensitivity are crucial. Their ability to bind with high affinity to specific antigens makes them ideal candidates for both therapeutic and diagnostic use.
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