Recombinant proteins are vital for many applications, including developing therapeutic drugs and enhancing food processing. They can also be used for protein engineering, high-throughput screening, and more. Historically, these proteins would be purified from animal sources, but recombinant protein expression offers advantages in supply and safety, allows for customization and engineering, and reduces batch-to-batch variations.

Why you need recombinant protein expression  protein production essentially involves adding the gene of interest to a host cell, expressing it and then collecting the resulting protein for further characterization. Although at a theoretical level this seems straightforward, dozens of things can go wrong along the way, such as poor growth of the host cell, inclusion body formation, and insoluble proteins.

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The system of choice should be determined by the origin of the target protein–Bacterial proteins are better expressed in bacterial systems, while mammalian proteins need to be produced in mammalian cells (Chinese Hamster Ovary, Human Embryonic Kidney). Additionally, complex eukaryotic proteins that require significant post-translational modifications should be expressed in plant, insect or yeast cells as they do not use animal derived reagents for cultivation and thus do not require extensive purification procedures [1].

The promoter used should be suitable for the particular protein being synthesised. For example, a strong promoter should be chosen to allow high product accumulation, while a cold-shock promoter is ideal for aggregation-prone proteins. It is also important to determine if the recombinant DNA sequence contains any synonymous codons as this will cause depletion of the low-abundance tRNAs and result in misincorporation of amino acids during translation, resulting in the formation of insoluble inclusion bodies.

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