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