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GST-tag refolding?


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#1 tatzilo

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Posted 17 March 2011 - 04:25 AM

Hiya,

a general question. IF a GST-fusion protein might be precipitated in inclusion bodies there are plenty of solutions to work out the problem.
One solution, which should not be the first, might be the denaturation and renaturation of inclusion bodies. I have plenty of
experience with short tags in this field. But I don't know whether the Glutathion-S-transferase can be refolded so easily that it still interacts
with the matrix and a successful purification is possible.

Did anybody try this so far?

Thanks for your reply!

#2 protolder

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Posted 17 March 2011 - 11:04 PM

Hiya,

a general question. IF a GST-fusion protein might be precipitated in inclusion bodies there are plenty of solutions to work out the problem.
One solution, which should not be the first, might be the denaturation and renaturation of inclusion bodies. I have plenty of
experience with short tags in this field. But I don't know whether the Glutathion-S-transferase can be refolded so easily that it still interacts
with the matrix and a successful purification is possible.

Did anybody try this so far?

Thanks for your reply!

Hola, to me, gst fusions are to facility solubility of fusion protein when shor tags fails, because gst is soloble, so if you have insolubilization problems will be due to the partner of GST. If you are experimented in expression, have you try a light induction to have poor expression but soluble. Buena suerte




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