Nicotiana Tabacum Expression System
Compared to conventional expression systems, such as microbial fermentation and mammalian cell cultures, plant production systems are inexpensive, easily scalable, free from human pathogens and offer the potential for direct oral administration.
Tobacco has the most established history for the production of recombinant proteins because it is readily amendable to genetic engineering and has a high biomass yield. Furthermore, the tobacco expression platform is based on leaves, which removes the need for flowering, significantly reducing the potential for gene leakage into the environment through pollen or seed dispersal. Most importantly, tobacco is a nonfood, nonfeed crop, which minimizes regulatory barriers by eliminating the risk of plant-made recombinant proteins entering the food chain.
Amongst different Nicotiana plants, Nicotiana tabacum produces the highest transient concentrations of recombinant proteins, in addition to producing a large amount of biomass and a relatively low quantity of alkaloids, thus making it the most effective plant host for recombinant protein production.
Profacgen has developed a novel Nicotiana tabacum specific expression platform for recombinant protein production at high purity. Recombinant protein expressed from plants generally possesses post-translational modifications, which are required for enhancing protein stability, bioactivity and favorable pharmacokinetics.
Features of Nicotiana tabacum Specific Expression Platform:
| High biomass yield and Minimal endotoxin level. | |
| High purity and Free from mammalian pathogens. | |
| Low-cost genetic engineering. | |
| Scalable production and downstream processing. |
At Profacgen, our unique technology increases the economic feasibility of the tobacco expression platform. A wide variety of therapeutically important recombinant proteins are produced at fast growth rates & high biomass yields and with high soluble protein levels & low alkaloid content.
Profacgen provides you with an ultimate solution of animal-free protein production. Our service can be tailored according to your specialized requirements (codon optimization, tag selection, purity etc.). Our expertise guarantees high protein quality, short turnaround time, and the best price in the market!
Reference: Conley, A. J., Zhu, H., Le, L. C., Jevnikar, A. M., Lee, B. H., Brandle, J. E. and Menassa, R. (2011), Recombinant protein production in a variety of Nicotiana hosts: a comparative analysis. Plant Biotechnology Journal, 9: 434–444. doi:10.1111/j.1467-7652.2010.00563.x