Does anyone have experience with using combination histidine and GSH
transferase fusion vectors for expression and sequential affinity
purification of the resulting fusion proteins through Ni and GSH agarose
resins? There are several such vectors on the market (i.e. Pharmingen),
but they claim their purpose in marketing them is for "customer
flexibility" rather than for providing a dual affinity purification
method. Has anyone tried to purify an expressed fusion protein using
both affinity methods? Any responses would be appreciated.
Steve Harwood
Dept. Agricultural Chemistry
Oregon State University
Corvallis, OR 97331
