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Make the most of PEGS US 2024 – Book a meeting with our team and start your journey to innovation!
90% success rate and above 1500 proteins expressed is the best demonstration of the quality of our protein expression service! What is our winning strategy for high yield protein expression? High performance proprietary protein expression systems, a team of protein experts and dedicated protein production platforms.
Skyrocket your protein expression
Try XtenCHOTM, the most performing protein expression system.
Wide range of mammalian expression systems
As a protein production expert, we propose CHO and HEK expression systems with different protocols and tools.
Large-scale production in a short timeline
Our cell culture can reach 20L per batch. Get multi-gram quantities of protein in 4 weeks!
From transient to stable protein expression
We propose a solution adapted to your requirements.
Protein expression experts
With 1500+ proteins and a success rate over 90%, our expertise has no equivalent.
Integrated solution from gene to protein
We take care of your project from gene synthesis to protein expression.
XtenCHOTM is the gold standard for protein expression. After many years of intensive research, ProteoGenix released an expression system able to outperform ExpiCHO, the current reference. Check some data on our recombinant antibody production page.
This is only one demonstration of the outstanding performance we can achieve with our proprietary protein expression system. Don’t miss the opportunity to skyrocket your protein production with XtenCHOTM!
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ProteoGenix strives at offering to its customers the most advanced protein production platforms. With XtenCHOTM and our GS deficient cell line, our experts developed their own tools to break the limits of your protein expression and to bring an adapted answer to all your challenges. Looking for short-term production of multi-gram amount of proteins? Need a cell line for long term recombinant protein production? Don’t go anywhere else, you are at the right place!
Rabbit IgGs demonstrate very high affinity and specificity. However, their very low productivity often limits their use (typical protein expression yield around 20mg/L). ProteoGenix is able to express these antibodies with yields over 200mg/L.
A CHO cell culture was transiently co-transfected with vectors coding for Rabbit IgG HC and LC. Cells were harvested 6-days post-transfection. Target antibody was purified by affinity.
Figure 1: Target mAb purification profile. Coomassie blue staining.
Non-reducing analysis.
MW. Molecular weight marker. IN. Input. FT. Flow through. W. Washes. E. Eluted fractions
After purification, fractions of interest were pooled and final samples were concentrated and buffer exchanged. A final QC of the protein expression was then realized by SDS-PAGE in reduced and non-reduced conditions.
Figure 2: Final QC of purified recombinant mAb. Coomassie blue staining.
2µg of sample loaded per lane
Multi-gram protein expression is a pre-requisite for many academic (for example functional analysis, crystal structure determination…) industrial and biopharmaceutical projects. For long, achieving high yields in recombinant protein productions using mammalian cells was considered as particularly challenging. Today, achieving yields over several grams per liters is regularly possible and thus overcomes the economic issues associated with the use of mammalian cell lines. These new advances in protein expression were encouraged by the fast increase of approved biotherapeutics expressed in mammalian cells.
More and more investments are made to develop biopharmaceuticals such as therapeutic antibodies or proteins. In this context, the use of mammalian cells for protein production is of particular interest.
The main difference between bacterial and mammalian cell lines comes from the presence of post-translational metabolic machinery. Thus, obtaining protein expression with proper glycosylation profiles is only possible with protein production in mammalian cells. This is particularly relevant for recombinant therapeutic antibody production where proper glycosylation can induce increased efficacy, stability and safety. In contrast, antibody fragments can be produced in bacterial expression systems.
Mammalian cells protein expression also allows for proper protein folding, a determining criteria to prevent the loss of biological activity.
To conclude, one of the main ideas to keep in mind is that recombinant protein expression in mammalian cells increases their compatibility for further human use. That’s why they are the reference expression systems when it comes to therapeutic antibody or protein production.
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