Hi, I need some information regarding protein folding. We are manufacturer of Human insulin and Human growth hormone. I would like to know some details on SDS page. Afte refolding and enzyme digestion we are processing for HIC and after that we are doing crystallization for final product. During the crystallization we seem to find some dimers present in our target protein. Can you please help me how to remove dimers in the target protein.
Lee You can try denaturing SDS PAGE. In case you get only single bands that will confirm homomers. If you get 2 bands of different sizes that add up to be around your protein MW that implies your protein is a heterodimer.