There are five immunoglobulin classes in humans. Out of these, immunoglobulin M (IgM ) is a high molecular weight protein that has five or 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.
Goat polyclonal anti-Human IgM (μ-chain specific)-Alkaline Phosphatase antibody is specific for human IgM when tested against human IgA, IgG, IgM, Bence Jones kappa, and lambda myeloma proteins. The conjugate shows no reactivity with mouse or rat IgG.
IgM is a glycoprotein with 5 n-linked glycosylation sites on the heavy chain. An ELISA assay was performed to identify glycosylated forms of IgM that bind to lectin. Alkaline phosphatase conjugated goat anti-human IgM was used as the secondary at 1:2000 and developed using p-nitrophenyl substrate (Sigma).
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.
Immunoglobulin M (IgM) antibodies appear early in the course of infections. IgM antibodies are responsible for agglutination of red blood cells in mis-matched blood transfusions. The level of IgM may vary with the status of disease or infection. Alkaline Phosphatase is an enzyme that catalyzes the conversion of chromogenic substrates such as p-nitrophenylphosphate (PNPP); chemiluminescent substrates such as CDP-Star® and fluorogenic substrates such as 4-methylumbelliferyl phosphate (4-MUP) into detectable chromophores, light-emitters or fluorescers, respectively.
No cross-reaction with mouse and rat IgG
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 and 15 mM sodium azide
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