Human IgM antibodies are glycoproteins that are mainly produced by the B-1 cells and regulate the physiology and growth of the human B cell reserve. Circulating monoclonal IgM antibody that binds to myelin-associated glycoprotein has been linked to the demyelination of peripheral nerves in humans . Anti-human IgM μ-chain specific−peroxidase antibody is specific for human IgM when tested against human IgA, IgG, IgM, Bence Jones κ and Lambda myeloma proteins.
There are five immunoglobulin classes in humans. Out of these, immunoglobulin M (IgM) is a high molecular weight protein that has five to six subunits. IgM monomers are made of two heavy chains and two light chains connected by a disulfide bond. Human serum shows low concentration of IgM monomers. It has a high carbohydrate content of about 12%. It is the first immunoglobulin produced by neonates.
Anti-Human IgM (μ-chain specific)-Peroxidase antibody has been used in direct binding assays to detect antiphospholipid antibodies (aPL).
Anti-human IgM (μ-chain specific)-Peroxidase antibody is suitable for use in direct ELISA (1:10,000 and 1:5000). It has also been used in indirect ELISA (1:2000). The concentration of IgM in supernatant samples was determined by ELISA using HRP-conjugated goat anti-human chain specific IgG as the secondary antibody. The antibody has also been used in Western blotting.
Immunoglobulin M (IgM) acts as an antigen specific part of the B cell antigen receptor on the surface of B lymphocytes that are not stimulated, in its monomeric form. Polymeric IgM molecules also serve as important activators of the classical complement cascade. IgM is essential in agglutination and cytolytic reactions.
Solution in 0.01 M phosphate buffered saline, pH 7.4 containing 1% BSA with preservative.
Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, Elsevier/North Holland Biomedical Press, Amsterdam, p215 (1978).
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