HUMAN IgM (myeloma) whole molecule

Human IgM (myeloma) whole molecule was prepared from human serum by a multi-step process which includes delipidation, selective precipitation and tandem molecular sieve chromatography followed by extensive dialysis against the buffer stated above.  Human IgM (myeloma) whole molecule was assayed by immunoelectrophoresis resulted in a single precipitin arc against anti-Human Serum and anti-Human IgM (µ chain specific).  No reaction was observed against anti-Human IgG F(c).  Some light chain cross-reactivity will occur with anti-Human IgG. Immunoglobulin M is the largest antibody isotype and the first to be secrected against an initial exposure to antigen. IgM is predominantly produced in the spleen. Formed from covalently linking 5 immunoglobulins together, the approixmate molecular weight of IgM is 900kDa and possesses 10 binding sites (though due to the size of most antigens, not all sites are capable of binding at once). Due to this large size, IgM is typically isolated to the serum.