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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.
Complement-dependent cytotoxicity (CDC) is an effector function of IgG and IgM antibodies.When they are bound to surface antigen on target cell (e.g. bacterial or viral infected cell), the classical complement pathway is triggered by bonding protein C1q to these antibodies, resulting in formation of a membrane attack complex (MAC) and target cell lysis.
Five sub-units come together to form a channel. Each channel consist of two alpha chain, one beta, one gamma and one delta chain.These five chains assemble together (along with certain receptors like protons or acetylcholine) forming the structure of the channel. [1]
The IgG, IgE and IgA antibody isotypes are generated following class-switching during germinal centre reaction and provide different effector functions in response to specific antigens. IgG is the most abundant antibody class in the serum and it is divided into 4 subclasses based on differences in the structure of the constant region genes and ...
Immunoglobulin therapy is the use of a mixture of antibodies (normal human immunoglobulin) to treat several health conditions. [13] [14] These conditions include primary immunodeficiency, immune thrombocytopenic purpura, chronic inflammatory demyelinating polyneuropathy, Kawasaki disease, certain cases of HIV/AIDS and measles, Guillain–Barré syndrome, and certain other infections when a ...
A pentamer is an entity composed of five subunits. In chemistry, it applies to molecules made of five monomers . In biochemistry, it applies to macromolecules, particularly pentameric proteins , made of five protein sub-units.
The J chain regulates the multimerization of IgM and IgA in mammals. When expressed in cells, it favors the formation of a pentameric IgM and an IgA dimer. IgM pentamers are most commonly found with a single J chain, but some studies have seen as many as 4 J chains associated to a single IgM pentamer.
mAbs is a peer-reviewed multi-disciplinary scientific journal established in 2009, published by Taylor & Francis and dedicated to the art and science of antibody research and development. Its editor-in-chief is Janice M. Reichert [1] and it is affiliated with The Antibody Society.