Antibodies, also known as immunoglobulins, are Y-shaped proteins that are produced by the immune system to recognize and neutralize foreign substances, such as viruses, bacteria, and toxins. They are an important part of the body's defense mechanism against infections and diseases.
Antibodies are made up of two heavy chains and two light chains that are linked by disulfide bonds. The tips of the Y-shaped structure are called the antigen-binding sites, which are responsible for recognizing and binding to specific antigens on the surface of foreign substances. The rest of the antibody, known as the constant region, interacts with other immune cells to trigger the elimination of the foreign substance.
Antibodies are generated by B cells, which are a type of white blood cell. B cells produce a diverse repertoire of antibodies through a process called somatic recombination, where segments of antibody genes are shuffled and combined to create unique antibody sequences. This allows the immune system to recognize a wide range of foreign substances.
At Biointron, we specialize in antibody discovery and development. Our high-throughput single B cell screening platform can screen millions of plasma B cells from immunized animals to identify rare, antigen-specific antibodies. We also offer a rapid and reliable recombinant antibody production service, which can provide you with a purified, guaranteed amount of recombinant antibody in just two weeks.
If you're interested in learning more about our antibody discovery and development services, please don’t hesitate to contact us.
The therapeutic efficacy of antibodies is closely related to their ability to recognize and bind specific epitopes on target antigens. Epitopes, or antigenic determinants, are a group of amino acids or other chemical groups that are part of a molecule to which an antibody attaches itself. Epitope characterization can help reveal the mechanism of antibody binding and apply intellectual property (patent) protection for novel antibodies, in addition to designing antibodies with high specificity and minimal cross-reactivity.
Understanding the differences between antibody specificity and selectivity is essential for designing and interpreting antibody-based assays in research for experimental accuracy and data interpretation. Antibody specificity refers to an antibody's ability to recognize and bind to a particular epitope—a unique part of an antigen that elicits an immune response.
Antibody-based assays are essential tools in biomedical research, providing the means to detect, quantify, and visualize specific proteins or antigens within complex biological samples. These assays' efficacy hinges on the antibodies' precise properties. While affinity, avidity, specificity, and selectivity are fundamental to antibody performance, the ultimate impact of these properties is heavily influenced by the experimental context in which the antibody is employed.
Biologics, particularly antibodies, have become indispensable in biomedical research and therapeutic development. Research-use-only (RUO) biologics play a pivotal role in preclinical studies, providing researchers with the necessary tools to explore antibody functions and therapeutic potential in vivo.
ScientistとScience Exchangeとのご利用可能です。
