Abstract
As a comparative study, the extracytoplasmic domain of human CD83 (hCD83ext) was expressed as a glutathione-S-transferase (GST) fusion in two Escherichia coli B strains, i.e., BL21 and Origami B, respectively, with a reductive and oxidative cytoplasm. The final therapeutic products of hCD83ext produced by the two expression hosts exhibited significant differences in protein conformation and molecular property, which presumably resulted from different disulfide patterns. The study highlights the importance of developing proper host/vector systems and biomanufacturing conditions for the production of recombinant therapeutic proteins with a consistent product quality.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
