I have produced a recombinant NRG egf-like domain, fused with His tag, by
E.Coli. I have extracted it from inclusion body using UREA.Then I have
purified it by NicKel colum and dialyzed.
Is the dialysis sufficient to renature my protein?
What can I do to optimize renaturation so that I can be sure to have my
protein in an active form? I need the EGF-like domain binds to his receptor.
Thank you very much!
lorenza
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