Selection of Recombinant Human Antibodies

Abstract

Since the development of therapeutic antibodies the demand of recombinant human antibodies is steadily increasing. Traditionally, therapeutic antibodies were generated by immunization of rat or mice, the generation of hybridoma clones, cloning of the antibody genes and subsequent humanization and engineering of the lead candidates. In the last few years, techniques were developed that use transgenic animals with a human antibody gene repertoire. Here, modern recombinant DNA technologies can be combined with well established immunization and hybridoma technologies to generate already affinity maturated human antibodies. An alternative are in vitro technologies which enabled the generation of fully human antibodies from antibody gene libraries that even exceed the human antibody repertoire. Specific antibodies can be isolated from these libraries in a very short time and therefore reduce the development time of an antibody drug at a very early stage.In this review, we describe different technologies that are currently used for the in vitro and in vivo generation of human antibodies.

Recombinant antibodies and their use for food immunoanalysis

“…In addition, the natural immune system imposes restrictions complicating the production of antibodies against unstable antigens, highly conserved proteins between species, or toxic compounds. Although researchers have tried to overcome these limitations by different strategies, including the generation of human antibodies in transgenic mice designed to produce a repertoire of human immunoglobulins followed by hybridoma, some of these caveats still persist [23]. The advantages, limitations, and key differences of different antibodies are presented in Table 1.…”