In the body, plasma B-cells produce large numbers of antibodies specific to foreign proteins. In the 1970s, studies into multiple myeloma (a B-cell cancer) revealed these plasma cells produced an antibody specific to one protein. This led to development of other antigen-specific antibodies.
In 1975 Kohler, Milstein et al produced the first monoclonal antibodies from a myeloma cell-line that had lost the ability to create immunoglobulins. These cells were fused with healthy antibody-secreting plasma spleen cells, producing a cell-line specific to one target area of the antigen – the first monoclonal antibodies. In 1988 Winter et al improved monoclonal techniques to make them suitable for human therapy use. At this time, the definitive work “Antibodies: A laboratory guide” was released. The generating and purifying methods used by antibody suppliers, like us at Novus Biologicals, remain much the same today as they were then.
Apart from the antigen-binding (V) sections, antibodies have a relatively uniform structure which allows them to be purified, tagged and detected easily, using generalised protocols. Despite technological advances, they continue to be the most specific and sensitive method of molecular detection today.
Antibodies are produced in either mono or polyclonal form, irrespective of class or subclass. Polyclonals are isolated and purified direct from the serum of the immunised animal. This results in a heterogeneous mix of proteins specific to the antigen, but varying in their target epitope. Monoclonal antibodies are derived from a cultured hybridoma cell-line, or peritoneal ascites fluid derived from the same source. Purification ranges from crude precipitation of sample protein mixes, to affinity purification of antibodies unique to a particular antigen molecule.
