Hello,
We are trying to purify an endogenous protein complex from tissue by
immunoaffinity column. We want to elute the complex in its native form
as intact as possible in the absence of the antibody. So far, we are
able to purify the full length protein of one subunit of this complex
in E. coli. We plan to generate polyclonal antibody against this
subunit and then make an affinity column. We plan to elute the complex
with the competition method using a lot of the E. coli purified
subunit. Since we have never done this kind of thing before, we are
wondering whether this approach sounds reasonable or not to the experts
out there.
Thanks.
Haibin Mao
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