Most of our recombinant proteins are produced in eukaryotic systems, but the certificate of analysis will provide you with the specific information on how individual products were produced.
Eukaryotes have several advantages as an expression system.
Eukaryotes inherently secrete very few native proteins, but they do secrete recombinant proteins. Therefore secretion is typically used as the first step in the purification process from a eukaryotic system. Recombinant proteins made in E. coli are often localized to inclusion bodies. Purification from inclusion bodies can require harsh conditions to free the recombinant protein, followed by subsequent refolding processes. These harsh treatments can negatively affect the function of the protein.
Recombinant proteins secreted by eukaryotes are processed by the Golgi apparatus, and thus they can be post-translationally modified. These modifications include glycosylation, phosphorylation and sulfation. There are many proteins that require modifications for protein function, proper folding or solubility.
Eukaryotes do not have a bacterial cell wall like E. coli, thus there is no endotoxin (lipopolysaccharide) present that can affect inflammatory responses in your target system.