Mapping Structural Proteins of Cultured Cells by Monoclonal Antibodies

Conventional antisera to purified antigens have proved to be very useful in the identification, quantitation, purification, and immunofluorescence localization of structural proteins of animal cells (Nishi and Hirai 1972; Goldstein 1976; Yalow 1978). Such antisera, however, usually contain a mixture of antibodies with different classes of immunoglobulins and different antigenic specificities. The monoclonal antibody techniques developed by Köhler and Milstein (1975) have provided a means by which antibody with constant specificity and uniform isotype may be obtained (for review, see Milstein 1980; Milstein and Lennox 1980). Moreover, the technique does not require a highly purified protein in order to raise a monospecific antibody to it. This advantage is particularly useful in raising monospecific antibodies to proteins that either exist in trace amounts or cannot be purified to homogeneity.