Problem:
I would like to conduct a simple demonization experiment for some protein I'm collecting from cultured cells. My thought is, that if I'm running a non-reducing, denaturing PAGE gel, then removing beta-mercaptoethanol /DTT from the sample buffer should be enough to allow di-sulfide bonds to form.
I have seen several authors incubate the cells first with a drug called BSS that diffuses across membranes and creates protein cross-links. I may be wrong, but the use of this drug seems more appropriate when trying to follow up with an immunoprecipitation or a pull-down assay.
If anyone has any experience with this statement, can you please explain to me?