Antibodies serve as both therapeutic and research tools due to their high specificity and low immunogenicity. Therapeutically, they target specific antigens to treat diseases like cancer and diabetes. In research, they aid in protein localization, isolation, and cell separation. Their reproducibility and scalability make them valuable, but the need for diverse antibodies necessitates ongoing discovery and testing. Limiting focus to human antibodies restricts availability, while chimeric and humanized antibodies expand the range to include non-naturally occurring types, enhancing their application and functionality. 

This technology is a chimeric antibody engineered by joining immunoglobulin M (IgM) fragments from humans and teleost fish, which does not encode a Joining-Chain (JC) to assemble polymeric immunoglobulins. The resulting structure is distinct from mammalian IgM. Receptor binding sections of the chimeric antibody are from the human sequences, and therefore they react with human antigens. This undiscovered chimeric class of human tetrameric antibodies widen the variety and potential applications of antibodies for therapeutic and research purposes.  

Lyu, M., Malyutin, A.G. & Stadtmueller, B.M. The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function. Nat Commun 14, 7583 (2023). https://doi.org/10.1038/s41467-023-43240-z [2]