Abstract
Recombinant human transforming growth factor β2 (TGF-β2) was cloned and expressed in E. coli. The protein was isolated from inclusion bodies, renatured and purified to a single component as judged by reversed-phase HPLC. The recombinant TGF-β2 was shown to have a biological activity equal to that of native TGF-β2 in a fibroblast migration assay. Pure, active recombinant TGF-β2 has been crystallized from polyethylene glycol 400. The trigonal crystals of spacegroup P3 121 or P3 221 have unit cell dimensions of a= b=60.6 Å, c=75.2 Å and diffract beyond 2.0 Å.
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.
