I want to reduce the volume of my eluate of protein complex by precipitation and resloving in small volume so I can load them into SDS-PAGE gel.The eluate comes from the elution of Strep-Tactin Superflow resin with elution buffer with 2.5mM D-Desthiobiotin in it.
The precipitation method should be able to precipitate each proteins in the former complex no matter the abundance is low or high.
The precipitation should be able to readily been resolved again without changing the profile of former composition of proteins.
Then what is your suggestion? As the TCA precipitation is hard to be resolved again.
PS:My overall purpose is to discover new interacting protein of protein of interest by Strep-Flag tandem purification.