Dear all,

after IMAC elution, my E. coli expressed protein (pI=6,32, MW=13 kDa) is in 400 mM Imidazol and 0,3 M KCl. TEV-Protease and cleaved off His-Tag are also swimming in this solution.

I want to purify further and use ion exchange for that, because it is a concentrating chromatographic step, perfect for recollecting my protein after refolding.

My refolding buffer has 2 M GHCl and 50 mM Arginine, will these interfere with ion exchange? I want to elute in pH 4.5 (protein most stable @ this pH)

Which resin type and which type of ion exchanger (strong or weak) would you propose?

Which strategy would you propose?

Thank you all for your input!

Kind regards,

Peter

More Peter Rehbein's questions See All
Similar questions and discussions