Production of human proteins using well-established and alternative recombinant expression hosts

In our work, we demonstrate using several approaches of production of a difficult-obtainable human lectin. We tried production of this protein using well-established E. coli expression host but this way failed because the protein is produced in the insoluble form only. Hence refolding, in vitro denaturation/renaturation and some solubility-enhancing tags were utilized to obtain protein in soluble form. Finally, it turned out that the L. tarentolae possibilities of the disulfide bond formation and the human-like glycosylation are crucial for a sufficient production of our target protein and it seems to be the very effective system for a routine production of human proteins in general.