Refolding a protein

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oppox
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Refolding a protein

Post by oppox » Wed Sep 27, 2006 11:54 am

Hello, I have a protein that has to be denaturated before purification. I have tried to refold it by quick dilution but then it aggregates again. My question is, should I try and refold it on the purification colonn (Ni, his-tag) instead (by slow dilution), is it a better way?

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