When we refold the protein by reducing the denature buffer, we always suffer from protein precipitate. Is it ok for using the rest of the soluble form to do a bioactive experiment and animal study?
yes.
you expect precipitation during refolding. The soluble fraction could very well be folded and active.
Just try.
Hi,
It is very rare to obtain 100% refolding efficiency. Just remove the precipitate with centrifugation and go on. But remember to check activity of your soluble fraction to confirm that it's properly folded.
As shared above, Centrifuge the sample and if required filter using 0.45Micron syringe filter and carry-out Circular Dichromism (CD) expt. with the protein sample to check if its folded properly and then go ahead with other experiments.
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