Recombinant Protein Therapeutics

Herbert Boyer first developed recombinant DNA in 1973, not knowing how his findings were going to transform the pharmaceutical and agricultural industries. Modern lab techniques and usages have taken recombinant proteins to a whole new level, and they are now widely used in various ways in many different industries.

What is a Recombinant Protein?

Recombinant DNA molecules are semi-synthesized molecules formed at the laboratory and are the result of the genetic recombination of DNA sequences from different sources (1). Recombinant DNA, also known as chimeric DNA, can be formed of sequences from different organisms.  Through a variety of techniques, scientists are able to join things like bacterial DNA with plant DNA to create a unique sequence that is not found in the genome and contains sequences of nucleic acids from the donor and the acceptor (1).

The traditional method, also used by Herbert Boyer, is to extract and cut up DNA from a donor into fragments containing one or several genes and then insert them individually into autonomously replicating DNA molecules such as bacterial plasmids. The recombinant plasmid acts as a vector that is then transferred into another bacteria by a process called transformation. The bacteria will subsequently divide and form a colony that will contain the new recombinant DNA (1). The mammalian immune system would typically destroy the plasmid, which is why viruses are frequently used to insert genes into the eukaryotic genome (2).

The application of recombinant proteins produced in the laboratory is increasing rapidly in biotechnology. Before their discovery in the seventies, proteins of interest were extracted from their natural sources through expensive processes (3).

Some popular examples of recombinant proteins include: the recombinant human insulin, to treat patients with diabetes, the recombinant human growth hormone, administered to patients with deficient pituitary glands, and the recombinant chymosin, in the production of cheese. These genetically engineered molecules inserted in a new host can make it possible for things like yeast to secrete human insulin which could, in turn, replace the need for animal sources of this hormone.

Recombinant Proteins Perspective

Technology is the key contributor to the improvement and the development of recombinant proteins. Better methods of purification, protein characterization and the invention of the PCR have given researchers the tools to better understand protein structure and behavior and the ability to develop molecules with better biological properties. Recombinant pharmaceuticals are attaining rapid commercial approvals due to the better biochemical, immunological and functional testing that laboratories are using in genetically modified products (4).

Even though recombinant products have brought huge advancement in human life and have lowered the cost of many medicines, they still face some of the same challenges they had when they first came into the market. Recombinant pharmaceuticals are being used more confidently (5), but the concept of genetically modified products is still controversial and the complexity involved in genetic engineering can cause reluctance in utilization. Regardless of these obstacles, recombinant proteins have improved the quality of life for many and will continue to improve as technology and research continues.


  1. Griffiths A, Miller J, Suzuki D. An Introduction to Genetic Analysis. 7th Edition. New York: W. H. Freeman; 2000.
  2. Van Craenenbroeck K, Vanhoenacker P, Haegeman G. Episomal vectors for gene expression in mammalian cells. Eur. J. Biochem. 267, 5665±5678 (2000) q FEBS 2000
  3. Rosano G, Ceccarelli E. Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol. 2014 Apr 17;5:172. doi: 10.3389/fmicb.2014.00172. eCollection 2014.
  4. Khan S, Ullah M, Siddique R, Nabi G, Manan S, Yousaf M. Role of Recombinant DNA to Improve Life. Int J Genomics
  5. Koths K. Recombinant proteins for medical use: the attractions and challenges. Curr Opin Biotechnology. 1995 Dec;6(6):681-7.

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