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Proteogenix – Recombinant protein production
Post Genomic – Protein production
The advent of genomics has revolutionized the industry of production of recombinant protein. The interest of the diagnosis, research, medicine, veterinary and industrial sectors is growing. The laboratories of recombinant protein expression must adapt to find ever more innovative techniques to produce and purify proteins from their customers as quickly as possible and with the highest yields possible. 
Proteogenix exploits every techniques and tricks to improve the yield, purity and folding either for production in E. coli (Escherichia coli), expression in yeast, expression in baculovirus / insect cells or production in mammalian cells (CHO, HEK293) in transient or stable system.
Expression conditions (tag, vector, bacterial strains …)
To do this, Proteogenix organized its laboratories to enable it to test in the shortest period of time, as many conditions for production and purification of recombinant proteins as possible. More solutions we have for varying parameters, the more we optimize the production of recombinant proteins (optimal conditions differ greatly from one protein to another).
Thanks to our extensive experience in the production of recombinant protein, we benefit from a large number of technical advantages providing the best chance of producing a protein in native form, with a good yield, good purity and proper folding. We are deeply involved in all stages of production from codon optimization, vector choice, tag choice, culture medium, additives, bacterial strains, induction temperatures, IPTG concentrations, purification types to refolding techniques (dialysis, buffer exchange, rapid dilution, on column refolding …) With an extensive experience of over 15 years in the expression of recombinant protein, our team provides advises and strategic insights on technical measures to be taken according to the type of protein and the client’s applications.
This flexibility and experience held by Proteogenix in the expression and purification of recombinant proteins is all the more important that requests often concern very poorly characterized proteins. It is therefore often impossible to rely on production tests already done. The key word is flexibility, which also derives from special and very specific equipment, enabling to vary a large number of parameters and to treat different samples simultaneously. Expression conditions are very different from one protein to another and the access to different expression systems represents a major asset for success in the field of recombinant protein production.
Tags: poly-Histidine, GST, MBP
The use of different expression vectors containing different tags: poly-histidine, GST, MBP or no tag, are part of the many possibilities proposed by Proteogenix. Proteins can be produced in the soluble fraction or in the pellets / inclusion bodies. In most cases, the goal is, to produce in native condition but where the protein is produced in pellets / inclusion bodies, the protein can be extracted and purified in denaturing condition. It is then possible to refold the recombinant protein either by dialysis or by rapid dilution (drip), or by making an on-column refolding.
Expression of recombinant protein and literature:
When data on prior testing of a protein expression and purification are available, either through customers’ experiments or through literature, it may in some cases be an excellent source of help in strategic decision making to produce a recombinant protein.