ResourcesBlogThe Role of Antibodies in Immunotherapy
The Role of Antibodies in Immunotherapy
Biointron2024-01-20Read time: 3 mins
Image credit: DOI: 10.1016/j.trecan.2022.01.008
Immunotherapy is a type of treatment that uses the body's own immune system to fight diseases, including cancer. One of the key players in immunotherapy is antibodies.
Antibodies, also known as immunoglobulins, are proteins produced by B-cells that play a critical role in the immune system. They are responsible for identifying and neutralizing foreign substances, such as bacteria and viruses, by binding to them and marking them for destruction by other immune cells.
In recent years, researchers have discovered that antibodies can also be used to target cancer cells. Antibody-based immunotherapies work by using monoclonal antibodies, which are antibodies that are made in the laboratory to target specific proteins on cancer cells. When the monoclonal antibodies bind to the cancer cells, they can trigger an immune response that leads to the destruction of the cancer cells.
At Biointron, we are dedicated to accelerating antibody discovery for the development of new immunotherapies. Our expertise in antibody screening, engineering, and production allows us to provide high-quality antibody services that are critical to the success of immunotherapy research.
Through our state-of-the-art manufacturing and automation process, we are able to deliver antibody products that meet international standards in terms of quality, purity, and potency. By working with us, our clients can rest assured that they are receiving the highest quality antibodies for their research and development needs.
As the field of immunotherapy continues to grow and evolve, we are committed to staying at the forefront of antibody discovery and production. With our expertise and dedication to quality, we are proud to play a key role in the development of new immunotherapies that have the potential to transform the way we treat cancer and other diseases.
Antibodies are versatile molecules that perform a range of effector functions, many of which engage different arms of the immune system. Their modes of action extend beyond simple antigen binding, enabling the activation of various immune mechanisms that lead to pathogen neutralization and clearance. These functions include blocking molecular interactions, activating the complement system, and linking the humoral immune response to cellular immune responses via Fc receptor engagement.
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In addition to isotypes and subtypes, antibodies exhibit genetic variation known as allotypes, which are polymorphic epitopes on immunoglobulins. These allotypic differences arise from allelic variations in immunoglobulin genes, causing certain antibody subtypes to differ between individuals or ethnic groups. The presence of these polymorphic forms can influence immune responses, particularly when an individual is exposed to a non-self allotype, potentially triggering an anti-allotype immune reaction.
In mammals, antibodies are classified into five major isotypes: IgA, IgD, IgE, IgG, and IgM. Each isotype is defined by the heavy chain it contains: alpha (IgA), delta (IgD), epsilon (IgE), gamma (IgG), or mu (IgM). These structural differences in the heavy chains determine the antibody's function, tissue localization, and role in the immune response. Furthermore, antibody light chains fall into two classes—kappa and lambda—with kappa being more common, though both exhibit similar functions despite differences in sequence.
