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Proteogenix – Protein expression in E.Coli, yeast, baculovirus or mammalian cells
E.Coli, yeast, baculovirus / insect cells or mammalian cells
The most commonly used system for expression and purification of recombinant protein is E. coli. Indeed, it is the simplest and fastest system for custom expression of a protein and at low cost. Bacterial cultures grow much faster than insect cells, mammalian cells or yeast. 
It is therefore easier and quicker to test a large number of different conditions. Production yields of recombinant protein are also generally much higher than in yeast, baculovirus / insect cells or mammalian cells. Expression of recombinant protein in E. coli (Escherichia Coli) is often a preferred solution proposed by Proteogenix when the final application requires large quantities of proteins such as crystallography and nuclear magnetic resonance (NMR) and no Post-Translational Modifications (PTM) are required.
Inclusion bodies
However, one of the problems laboratories of recombinant protein production like Proteogenix have to cope with when using E. Coli is that the protein is often found in inclusion bodies as insoluble. More rarely, some proteins have very low expression level or no expression at all.
Post-Translational Modifications (PTM)
In cases where post-translational modifications are required in recombinant proteins produced in order to obtain enzyme activity or proper folding, we prefer to use an eukaryotic production system such as yeast, baculovirus / insect cells or mammalian cells. The choice of the system depends ultimately on the nature of the protein to produce and the application in which the expressed recombinant protein will be used.
Thanks to our know how in all these systems, Proteogenix is able to produce any type of recombinant protein of bacterial or fungal origin, nematodes, parasites and viruses, as well as plant and animal protein, including mammalian proteins and of course human proteins.
From gene to protein
With the combination of advanced molecular biology and chemical synthesis of oligonucleotides, it is now possible to obtain synthetic DNA fragments of several tens of kilobases. This allows Proteogenix to synthesize almost any gene or cDNA for the production of a recombinant protein. Moreover, in order to optimize the protein production yield, it is possible before gene synthesis to optimize rare codons for the selected expression system. Indeed, some proteins are very weakly expressed outside their natural environment because of rare codons poorly complementary with little pools of tRNA present in the host used for expression of recombinant protein. Rare codons modification is a very powerful tool that offers Proteogenix to improve production yields whatever the system used: E. coli, baculovirus / insect cells, yeast or mammalian cells.
Cloning
No matter which system is used for recombinant protein production, it is necessary that Proteogenix clones the optimized gene into an appropriate expression vector.