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anti-Immunoglobulin M (IgM) secondary antibodies

Immunoglobulin M (IgM) is constructed of five or six units (i.e. mostly as pentamers but also hexamers occur) which are each comprised of two heavy-chains (mu-chains) and two light chains, bound together by disulfide bonds and a so-called J-chain. A J-chain is usually, but not always, found in pentameric IgM but not in the hexameric form. It is not yet clear if pentamers without the J-chain fullfill different functions. Each monomer has two antigen binding sites, hence a pentameric IgM has 10 binding sites. IgM is by far largest antibody in the human circulatory system. In its pentamer form IgM has a molecular mass of approximately 900 kDa.

IgM is present on B cells and its main function apparently is the control of B-cell activation. Interestingly, it is also the primary antibody against A and B antigens on red blood cells and responsible for the blood-clotting reaction during blood-transfusion from wrong donors.

IgM is primarily found in serum and due to its size, it cannot diffuse well, and is found in the interstitium only in very low quantities.

The table below contains a selection of anti-IgM secondary antibodies:

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