The study of antibodies has been one of the focal points in biology and medicine for over 20 years. Monoclonal antibodies now constitute the most rapidly growing class of human therapeutics and have profoundly modified the treatment of a number of indications including cancer and autoimmune diseases.
One of the most established methods for the production of monoclonal antibodies is through the generation of myeloid myeloma cells lines, although more recently the selected lymphocyte antibody method has also become increasingly popular. One problem associated with these techniques is the rapid and accurate identification of the resultant antibodies. The screening of cell-culture supernatants for specific antibodies can be a tedious, time-consuming process and especially problematic when screening for low-abundance antigens, e.g., cell-surface proteins.
Traditionally, ELISA has been used for antibody screening but with numerous wash and incubation steps these assays are also time-consuming. Quantification of cell-surface proteins is also difficult using this method, primarily due to their low abundance and dependence on cellular expression.
Homogenenous mix-and-read assays overcome these problems. These simplified protocols involve the simultaneous addition of all assay constituents to one well, with the analysis performed once equilibrium has been reached, making these assays rapid, robust, and suitable for automation.
Automated mix-and-read assays for antibody screening were originally enabled by a cellular detection instrument that was based on fluorometric microvolume assay technology. Although this instrument has been discontinued, there remains a requirement for a system that is able to perform high-throughput, robust assays for antibody discovery.