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Recombinant Proteins In Research

Proteins play an integral role in human health. As such, basic, applied, and clinical research aims to understand how protein expression, localization, post-translational modifications (PTMs), and interactions regulate homeostasis and disease.

Our current understanding of how proteins affect cell phenotype is based on various applications such as affinity purification, Western blotting, and in vitro functional assays.  

Many of these techniques use recombinant proteins or proteins expressed in exogenous host systems. You can also check out Boster Bio featured products to know more about recombinant proteins.

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How are recombinant proteins made?

The first step in obtaining a recombinant protein is to synthesize the desired gene. It is important to consider the sequence of nucleic acids because amino acids are encoded by different sequences of 3 nucleic acids called codons.

For example, four codons (CTT, CTC, CTA, CTG) are translated into leucine amino acid residues. The translational efficiency of the protein is enhanced by optimizing the nucleic acid sequence reflecting the codon bias (due to the varying mRNA pool) of the selected expression system.

The synthesized gene is then cloned into a viral expression or vector. The expression vector is a plasmid cDNA containing the promoter sequence and the antibiotic resistance gene.

There are also frequent sequences at the N- or C-terminus that encode fusion markers for purification or identification of downstream proteins. Antibiotic resistance genes allow the selection of plasmid-carrying cells in antibiotic-based media. The viral vector encloses the desired gene with the viral sequence, ultimately causing the gene to be permanently inserted into the host chromosome.