As a key tool in Advantages of recombinant antibodies protein-detecting applications, antibodies have the potential to yield misleading results or even completely invalidate a study’s conclusions. Several older life science publications using catalogue antibodies derived from animals demonstrate such variability, leading to embarrassing retractions1 and product withdrawals2. The advent of recombinant antibodies has compensated for these limitations in the laboratory.

Recombinant antibodies are synthesised in vitro through recombinant genetic engineering/ display technologies (such as phage display, yeast display, or mammalian cell display), providing a powerful alternative to polyclonal and monoclonal antibody production methods based on animal immunization.

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Recombinant antibodies are produced in a controlled environment, improving consistency and reproducibility. They also do not contain unspecific serum components, which can reduce the purity of traditional hybridoma antibody production1.

Molecular biology cell culture techniques are scalable to industrial-relevant plant sizes, and can be used for large-scale recombinant antibody production, offering greater efficiency and cost savings1.

A recombinant antibody’s gene sequence is known, so it can be easily cloned into expression vectors to optimise cell growth and antibody yield. In addition, specialised media additives can improve cell viability and antibody expression levels.

Recombinant antibodies can also be engineered to have additional functionalities such as tags for purification or immunoprecipitation, conjugation sites to enable ligands to be attached, or mutagenesis to map the determinants of antigen recognition. In addition, recombinant antibodies can undergo in vitro affinity maturation campaigns to select Abs with increased specificity and reduced off-rates21.