Recombinant Protein Expression in E.coli 

If you need both, your recombinant protein and a corresponding antibody, our guaranteed antibody package will be the best service choice for you.

Our standard priority shipment will be on dry ice. If required, we offer shipment on blue ice, at -20°C or even at room temperature (lyophilized proteins only) as well.

We can additionally offer sterile filtration if you require this service.

E.coli is a widely used host for protein production due to its cost-effectiveness, especially when scaling up to larger production volumes. The expression processes are typically fast, straightforward and can be easily and economically scaled up. This makes E.coli an efficient choice for many applications.

Yes, eukaryotic proteins can be synthesized in E.coli. However, certain limitations may arise due to the need for post-translational modifications such as glycosylation, complex folding processes and the formation of physiologically correct disulfide bonds. These factors can impact the successful production of a functional target protein.

One key advantage of E.coli as a Gram-negative bacterial host is its ability to secrete proteins into the periplasmic space, which provides an oxidizing environment that promotes the correct formation of disulfide bonds. This can enhance proper protein folding and solubility, making it a cost-effective and efficient strategy for producing structurally complex or even eukaryotic proteins in E. coli. Additionally, periplasmic secretion can be a promising approach for expression of challenging or potentially toxic targets.

Yes, co-expression in E.coli allows the production of heterodimers, oligomers, and multiprotein complexes, enabling the synthesis of more complex target architectures. Furthermore, co-expression of enzymatically active interaction partners can facilitate specific modifications, such as targeted biotinylation of recombinantly produced proteins. The co-expression of molecular chaperones or folding helpers can also improve the solubility and stability of complex target molecules.