The described procedure consists in forming a precipitate of a single protein immediately after its separation by electrophoresis by the respective mono-specific antiserum. The remaining proteins, unifixed, are removed by  washings and therefore, after the staining it is possible make a direct comparison with the reference pattern. Each used electrophoretic membrane will allow the complete sample identification. The monoclonality recognition of an immunoglobulin homogeneous by the electrophoretical point of view is based upon the demonstration that the protein is composed by the same type of heavy and light chains. Consequently, the most monoclonal component identification is obtained using the five antisera against IgA, IgG, IgM, Kappa and Lambda. The suggested procedure, due to the use of diluted mono-specific antisera, allows to perform the antigen antibody contact by diping the electrophoretic membrane directly into the antiserum, allowing the complete contact and avoiding uncomfortable incubations into the humid chamber.