The advent of biotechnology has made it possible to overcome the undesired host antiglobulin response evidenced following the injection of rodent antibodies for radioimmunoimaging; initially through the construction of chimeric and CDR-grafted antibodies and more recently through the derivation of completely human antibodies. Available platforms for derivation of completely human antibodies include phage- and ribosome-display techniques and transgenic mice that are deleted in their own antibody genes and reconstituted with large parts of the genes encoding for human antibodies. Additionally, biotechnology has made it possible to tailor affinity, respectively through CDR-walking or chain schuffling, and avidity, respectively through manifold engineering, of antibodies and derivatives. More recent developments include the development of highly stable single domain binders based on the use of a conserved framework region and a highly variable antigen-binding site, using other proteins or molecules that are smaller in size and easier to manufacture than antibodies. Finally, novel technologies have been and are being developed optimizing the concept of pretargeting.