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Immunoglobulin M (IgM) is the largest of several isotypes of antibodies (also known as immunoglobulin) that are produced by vertebrates. IgM is the first antibody to appear in the response to initial exposure to an antigen ; [ 1 ] [ 2 ] causing it to also be called an acute phase antibody.
This is a recombinant monoclonal antibody to IgM. The anti-antibody functions in early detection of antigens in serum rather than interstitial fluids. [13] Anti-IgM [B481] This is a recombinant monoclonal antibody to IgM. It is recommended to use anti-IgM [B481] as a secondary antibody against IgM primary antibodies. [14]
As IgM antibodies are expressed early in a B cell response, they are rarely highly mutated and have broad antigen reactivity thus providing an early response to a wide range of antigens without the need for T cell help. [5] IgD isotypes are expressed on naive B cells as they leave bone marrow and populate secondary lymphoid organs.
Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.
This region allows antibodies to activate the immune system, for example, through binding to Fc receptors. In IgG , IgA and IgD antibody isotypes , the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains ; IgM and IgE Fc regions contain three heavy chain ...
The associated anti-A and anti-B antibodies are usually IgM antibodies, produced in the first years of life by sensitization to environmental substances such as food, bacteria, and viruses. The ABO blood types were discovered by Karl Landsteiner in 1901; he received the Nobel Prize in Physiology or Medicine in 1930 for this discovery. [ 5 ]