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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 antigen-binding assay, Western blotting, and/or ELISA, the antibody reacts with the light chains on mouse IgG and with those common to other mouse immunoglobulins. Reaction is primarily with kappa light chains. The antibody does not react with the heavy chain of mouse IgG. The antibody has been tested by ELISA to ensure minimal cross-reaction with bovine, goat, horse, human, rabbit, rat and sheep immunoglobulins, but it may cross-react with immunoglobulins from other species.