Resources Blog Antibody Isotypes: IgM

Antibody Isotypes: IgM

Biointron 2024-01-20 Read time: 3 mins
IgM.jpg
Image credit: DOI: 10.3389/fimmu.2020.01943

Immunoglobulin M is the first isotype to be expressed by the adaptive immune system in response to a foreign pathogen, during B cell development. It is typically present as the antigen receptor on the naïve B-cell surface, allow for the B cell to associate with the polypeptides CD79a and CD79b, which play roles in IgM cell signaling.

IgM is monomeric when first produced by plasma cells but when secreted can link to other IgM units to form a pentameric configuration containing a polypeptide J-chain. This occurs during maturation and antigenic stimulation and increases IgM’s avidity since there would be ten antigen-binding sites per pentameric molecule. Through interactions with the antigen, IgM can then opsonize it for destruction.

The detection of IgM can be used to diagnose patients from acute exposure to a pathogen, since IgM is typically linked with a primary immune response. However, it does not indicate whether the patient still has that pathogen or if it had been eliminated, since memory plasma cells help form immunological memory to generate antibodies against a pathogen for many more months and years to come.1

In addition, several disorders can be connected with IgM, such as X-linked Hyper-IgM Syndrome. This is a rare primary immune deficiency disorder, characterized by elevated IgM levels but deficient levels of other immunoglobulin isotypes, as well as defects in cellular immunity. Other disorders linked to IgM include Selective IgM Deficiency, Cold Agglutinin Disease, and Monoclonal Gammopathies.2

At Biointron, we are dedicated to accelerating your antibody discovery, optimization, and production needs. 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. 


References: 

  1. Schroeder, H. W., & Cavacini, L. (2010). Structure and Function of Immunoglobulins. The Journal of Allergy and Clinical Immunology, 125(2 0 2), S41. https://doi.org/10.1016/J.JACI.2009.09.046 

  2. Sathe, A., & Cusick, J. K. (2022). Biochemistry, Immunoglobulin M. StatPearls. https://www.ncbi.nlm.nih.gov/books/NBK555995/

Subscribe to our Blog

Recent Blog

Computational antibody methods schematic. DOI: 10.1093/bib/bbz095The development of therapeutic antibodies has been significantly enhanced by advancements in computational methods and artificial intelligence (AI). These technologies have streamlined the antibody discovery process, improving the abil

May 27, 2024
Blog

Welcometo Antibody Basics by Biointron,Part 8. In this episode, we’ll talk about therapeutics targeting cancer.What is cancer immunotherapy?Cancer immunotherapy leverages the body's immune system to fight cancer more selectively and effectively than traditional methods such as chemotherapy

May 24, 2024
Blog

The generation of an immune response to a vaccine. DOI: 10.1038/s41577-020-00479-7Vaccination is one of the most effective tools in preventing infectious diseases. At its core, the success of a vaccine hinges on its ability to induce a robust and lasting antibody response against a specific pathogen

May 22, 2024
Blog

Innovation orientation and goals for transforming CAR-T cell engineering. DOI: 10.1186/s13045-020-00910-5Chimeric antigen receptor (CAR)-T cell therapy is a revolutionary cancer treatment in which engineered CARs redirect lymphocytes, typically T cells, to recognize and destroy cells expressing a sp

May 20, 2024
Blog

Our website uses cookies to improve your experience. Read our Privacy Policy to find out more.