Abstract
The two-domain form of recombinant soluble human CD4 (rsCD4 183) has been used for structural studies and to probe the interaction of CD4 with its ligands. rsCD4 183 has generally been produced in Escherichia coli in the form of inclusion bodies. The generation of conformationally native protein from these inclusion bodies is a time-consuming and inefficient process, requiring a refolding step. Here, we describe a procedure for producing 2–4 mg of secreted, conformationally native rsCD4 183 per liter of E. coli, completely bypassing the requirement for protein refolding in vitro. Furthermore, the yield of active protein is comparable to that reported for expression systems that generate inclusion bodies.
Sign-in/Register to access full text options 
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
