Production of human proteins using well-established and alternative recombinant expression hosts
2014
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.
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