SOLUBLE PROTEIN EXPRESSION SERVICES

What Makes our Soluble Protein Expression
Service so Different?

Each project is unique! With five different expression systems, ProteoGenix creates custom solutions to meet your goals. Each protein expression project includes an optimization phase, where several parameters are tested at a small-scale to guarantee a successful protein expression project.

With more than 7000 successful soluble protein expression projects and more than 28 years of experience, you can count on our team to overcome your most difficult challenges.

Strategies to Optimize Recombinant
Soluble Protein Expression Yields

Thanks to continuous advances in the biotechnological field, recombinant protein expression proved its efficiency as a versatile tool in research as well as in innovative drug discovery. In this context, higher production efficiencies are needed to fulfill the increasing demands on this market. Yet, overexpressed proteins can be challenging as they tend to form insoluble aggregates, so-called inclusion bodies. This phenomenon usually correlates with the loss of protein activity and poor yields.

Today, several protein expression hosts are available (bacterial, yeast, insect, mammalian). However,E.coli is usually the most used expression system. The latter constitutes an easy and inexpensive factory along with its ability to provide high yields. On the other hand, E.coli and other bacterial expression systems tend to form insoluble aggregates due to poor protein folding. For this reason, some industries prefer using mammalian cells to limit this side effect when it comes to complex proteins.

Here are some common methods to enhance protein solubility and yields in both eukaryotic and prokaryotic systems:

• Solubilization of inclusion bodies: Inclusion bodies are the only form of proteins that can be regenerated into their native and active form. It is possible to obtain soluble proteins from inclusion bodies by applying the denaturation and refolding method.
• Culture temperature: This method is frequently employed with E.coli. The aim is to reduce the formation of inclusion bodies by lowering the culture temperature. This was proven to boost the expression of chaperone proteins promoting the correct folding of the targeted protein.
• Transfection rate: 3 parameters contribute to modulating a protein’s solubility: Transfection agent concentration, induction time, and plasmid concentrations. Lowering concentrations and transfection time reduces the transcription and translation rates. Therefore, limiting the formation of aggregates and increasing protein solubility.
• Molecular weight: Proteins with molecular weights above 60kDa tend to decrease solubility in bacterial systems. In this case, it is better to privilege a mammalian expression system as they are more suitable for complex proteins.
• Cell strain: Since each protein is different, production can differ from one strain to another. Accordingly, it is recommended to test several strains and select the best fitting for the protein production strain with improved solubility rates.
• Media: Media composition is important for protein folding and solubility. The culture media should contain all the nutrients required for your protein expression throughout the process.
• Solubility tags: Solubility tags are peptide sequences fused to the targeted protein. They are used to enhance protein solubility but also to improve protein purification. The mechanism of action of solubility enhancement tags remains unclear till today; however, two hypotheses can explain these findings:
  • Solubility tags promote protein folding by attracting chaperones.
  •  Solubility tags exhibit electrostatic repulsion thanks to their highly acidic properties.

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