Protein Expression and Purification
As the mechanism for the scale synthesis and isolation of your targets, expression and purification are vital steps in efficiently elucidating proteins. We have comprehensive knowledge in four subtypes of expression systems: bacteria, yeast, insect, and mammalian. Factors including but not limited to protein mass, quantity demanded, modifications required, and functionality play a role in selecting the optimal system. Features for each are summarized below.
Most widely adopted and cost efficient. Very short doubling times with simple culture conditions (20 minute doubling time with ~10% mass/protein ratio). Plasmid design allows for wide use cases. These systems can have drawbacks in properly folding mammalian proteins and are prone to the formation of inclusion bodies.
Benefits from increased plasmid specificity. Quick doubling time (90 minutes), low culture cost. These systems can be used to produce both intracellular and extracellular proteins, and demonstrate some post translational modifications. Yeasts do not produce as much product and are liable to hyperglycosylation.
Demonstrates mostly proper folding compared with mammalian cells at an average 18-24 hour doubling time. Advantages in high cell density with complex post-translational modifications. Expensive and complicated culture relative to microbial lines with simplistic N-linked glycosylation.
Features all post-translational modifications with proper protein folding. Transient and stable expression by transfection. Slow, (average 24-hour) doubling time, with complex culture conditions and higher cost compared to other expression systems. Production efficiency variable, g/L yields are possible.