A second major milestone occurred in 1975 when Köhler and Milstein developed the hybridoma technology, enabling the production of high quantities of monoclonal antibodies of the desired specificity ( 2). This principle of immunodetection was first demonstrated in 1959 when Berson and Yalow developed the first radioimmunoassay for human insulin using a guinea pig antiserum ( 1). While most analytical methods rely on the separation of the analyte, the exquisite specificity of antibody recognition allows the detection of trace amounts of the target analyte even in highly complex matrices. Here, we critically reviewed each of these properties and highlight their relevance with regard to recent developments in different fields of immunosensing applications. These attributes include comprehensive representation of the immune specificity in display libraries, easy adaptation to high-throughput screening, exceptional stability, minimal size, and versatility as affinity building block. The recombinant form of their variable domain has outstanding properties that make Nbs, not just an alternative option to conventional antibodies, but in many cases, these properties allow them to reach analytical or diagnostic performances that cannot be accomplished with conventional antibodies. Even so, this does not seem to limit their specificity and high affinity as HcAbs against a broad range of structurally diverse antigens have been reported. With just three CDRs in their variable domains, the antigen-binding site of camelid heavy-chain-only antibodies (HcAbs) has a more limited structural diversity than that of conventional antibodies. Cátedra de Inmunología, Facultad de Química, Instituto de Higiene, UDELAR, Montevideo, Uruguay.
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