6His protein

alex emil kentsis aekentsi at midway.uchicago.edu
Thu Jan 29 09:39:32 EST 1998

i would suggest titrating the protein to determine what groups are being
ionized in order to solubilize it. the first hypothesis is that it's
rather hydrophobic and needs extensive ionization to be solubilized.
add 1 M guanidine hydrochloride and see if it helps.

M.H. Spronk (henri.spronk at bioch.unimaas.nl) wrote:
: 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

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