Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective.
Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc5µ portion of the human IgM heavy chain but not with human IgG, IgA, or the light chains of human immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine serum proteins, but it may cross-react with IgM from other species.
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