When collecting cell lysates for a Western blot, how do I induce di-sulfide bonds?
For the introduction of new cystine bonds, you will probably need to maintain an appropriate redox potential when dialyzing your cell-lysate to allow your cystine bonds to reform. To break the current di-sulfide bonds, we have been adding in Disulfide Bond Isomerases (DsBC to be precise) which will allow your lysate to get to an appropriate equilibrium.

As for examining for disulfide bond formation that has already occured between proteins in your lysate, removing reducing equivalents like DTT and beta-mercaptoethanol should do the trick. You can even denature your proteins by incubating them in LDS or Laemmli buffer at 90C as those components will not reduce your cystine bonds. In our experience the bands typically run at the expected molecular weight on a SDS-PAGE.