Immunoglobulins (antibodies) are composed of two identical heavy chains (H) and two identical light chains (L). This arrangement creates distinct regions, including the variable (V) regions responsible for antigen binding and the constant (C) regions that determine the antibody's class and effector functions. Immunoglobulins are vital components of the immune system, recognizing and neutralizing bacteria, viruses, and other pathogens. They are synthesized by B lymphocytes and exhibit several key features enabling them to function against infections. Immunoglobulins firstly exhibit a large diversity in their structure. Structural diversity arises from a genetic process occurring during B cell development in which each B cell produces a unique immunoglobulin receptor recognizing a specific antigen. This specificity ensures that the immune system can recognize a large range of potentially pathogenic antigens. The variable regions of immunoglobulins contain the antigen-binding sites specific for a particular antigen. Immunoglobulins are categorized into different classes (IgM, IgG, IgA, IgD, and IgE) based upon their distinct constant region. Each class of antibody has distinct functions and roles in the immune response. For example, IgM is the first antibody produced during an immune response, whilst IgG is involved in longer-term antigen recognition and is responsible for the B cell memory response. Conversely, IgA antibodies are abundant in mucosal surfaces, such as the respiratory, gastrointestinal, and urogenital tracts. At such locations they help prevent pathogens from attaching to mucosal cells and crossing into the body. IgA also plays a role in the new-born’s protection through breast milk. Finally, IgE antibodies are involved in most allergic responses. When the immune system overreacts to normally harmless substances, such as pollen or certain foods, IgE antibodies trigger the release of histamines and other inflammatory mediators, leading to allergy symptoms. Immunoglobulins also have various applications in medical diagnostics and therapies. They are used in tests to detect the presence of other antibodies as markers of infections or autoimmune diseases. Moreover, monoclonal antibodies, derived from a single B cell clone, have been developed for targeted therapies against various diseases, including cancer and autoimmune disorders. Immunoglobulins can trigger various immune responses through their constant regions. For example, IgG antibodies can activate the complement system, a group of plasma proteins that aid in pathogens inactivation, or facilitate opsonization, whereby antibodies bind to and tag pathogens for phagocytosis. Upon antigen encounter, B cells can undergo class switching, where they change the constant regions, producing antibodies with different effector functions. Finally, one of the primary functions of antibodies is to neutralize pathogens by blocking their ability to infect host cells. Such neutralizing antibodies can bind to surface viral proteins or other pathogenic molecules, preventing them from interacting with host cell receptors and thereby inhibiting infection. For example, several monoclonal antibodies have been developed commercially that can neutralize the surface spike protein of the SARS-CoV-2 virus, responsible for COVID-19. This protein is a key target for neutralizing antibodies since it is involved in the virus's entry into host cells by binding to the ACE2 receptor. We provide a wide product range of research reagents for investigating immunoglobulins, including IgG antibodies, IgM antibodies, IgA antibodies, TLR2 ELISA Kits, and EPO Receptor ELISA Kits. Explore our full immunoglobulins product range below and discover more, for less. Alternatively, you can explore our Heavy Chain, Receptors, and Light Chain product ranges.