After expression (in E.coli) of a recombinant human protein as part of a
6His-DHFR-fusion protein and purification using a Ni-NTA-column, the
protein is insolluble. The protein is soluble in a solution of pH 12, but
not at 7.5. Does anybody have experience with protein solubillization?
H.M.H. Spronk
Department of Biochemistry
University Maastricht
The Netherlands
henri.spronk at bioch.unimaas.nl
