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With more than 20 years of experience in custom protein production services and over 1,500 proteins successfully produced across 5 expression systems, ProteoGenix is a leading protein production company for difficult-to-express recombinant proteins and antibodies.
With more than 20 years of extensive experience in custom protein expression, and over 1,500 proteins successfully produced in 5 systems, ProteoGenix is a leader in difficult-to-express recombinant proteins and antibody production.
End-to-end protein production services designed to optimize yield, functionality and scalability for any recombinant protein.
Generate up to 2 mg of dozens of biologics with our high-throughput protein production platform.
Produce mg to gram-scale of recombinant protein using optimized transient expression systems.
Improve protein expression conditions and scale your production from grams to kilograms using bioreactors or stable cell lines.
Share your protein target and receive a tailored production strategy from our scientific team.
Choosing the right protein expression system is critical for yield, folding, solubility, activity and post-translational modifications.
Mammalian cells are ideal for complex eukaryotic proteins needing native folding and PTMs, and for low-endotoxin in vivo use.
E. coli is the go-to system for fast, high-yield expression of simple proteins, especially for structural biology.
Bacillus subtilis is a strong choice for secreted proteins, enabling easier purification from the culture medium.
Insect cells deliver high yields for large or complex proteins, with eukaryotic processing including glycosylation.
Yeast balances high expression with eukaryotic PTMs, suitable from small- to large-scale production.
If yield or activity is suboptimal, screen up to five expression systems to find the best fit fast.
| Mammalian Cells | E. Coli | B. Subtilis | Baculoirus/Insect Cells | Yeast (P. Pastoris, S. Cerevisiae) | |
|---|---|---|---|---|---|
| Time | 3-5 weeks | 2-3 weeks | 2-4 weeks | 6-9 weeks | 5-7 weeks |
| Post-Translational Modifications possibilities | High | Low | Low | Intermediate | Intermediate |
| Disulfide bond formation | +++ | ∅ | ∅ | ++ | + |
| Multi-domain and complex proteins expression capacity | +++ | ∅ | ∅ | ++ | ++ |
| Endotoxin Levels | Low | High | Low | Low | Low |
| Complexity for scale-up | Intermediate | Simple | Simple | Complex | Intermediate |
| Secretion level of the protein of interest | High | Low | Intermediate | Intermediate | Intermediate |
| Price | +++ | + | ++ | ++ | ++ |
Whatever your protein target, our broad technology platform is designed to overcome any expression challenge. With five expression systems, we maximize your chances of success. Our proprietary mammalian platform, XtenCHO® Race, is the highest-performing cell lines on the market, delivering robust yields and consistent quality.
” I recently chose ProteoGenix to produce a recombinant protein in HEK293 cells. The high productivity and strong activity of the protein obtained, probably due to proper glycosylation and folding, allowed us to generate exciting results in functional studies and reach new milestones in our research project. The quality of the service provided, and the smooth and kind communication I had with the account manager in charge of our project, were paramount to this success. I’m happy to recommend ProteoGenix for recombinant protein productions. “
Alvarado-Marchena, L., Martínez-Pérez, M., Aparicio, F., Pallas, V., & Maumus, F. (2022). Recent acquisition of functional M6A RNA demethylase domain in orchid TY3/Gypsy elements. Frontiers in Plant Science, 13. https://doi.org/10.3389/fpls.2022.939843
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Noack, L. C., Bayle, V., Armengot, L., Rozier, F., Mamode-Cassim, A., Stevens, F. D., Caillaud, M., Munnik, T., Mongrand, S., Pleskot, R., & Jaillais, Y. (2021). A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants. The Plant Cell, 34(1), 302–332. https://doi.org/10.1093/plcell/koab135