| | Re: How would immunoprecipitated proteins look like in an SDS-page experiment?
The immunoprecipitated (IP) proteins' migration in the gel should be delayed in comparison to non-IP proteins. This because the bound antibody causes an increase of the molecular weight of the IP protein thus delaying its migration.
However, SDS-page electrophoresis needs denaturation (boiling) of the proteins prior running. This will also denature the bound antibody and you will see two bands (one of your target protein and one of the antibody) instead of one; in which case the delaying won't be seen.