IDENTIFICATION OF PROTEIN-PROTEIN INTERACTIONS

APMS Solutions

Do you need more than just a list of proteins?

Using affinity purification methods such as immunoprecipitation enables the isolation of whole protein complexes from a cell or tissue extract. In the old days, or in workflows where knowing the identity of only one protein is needed, the immunoprecipitated proteins would be resolved by SDS-PAGE, stained, and individual bands were cut and analyzed by LC-MS/MS. With modern instruments, the whole protein complex can be subjected to proteolytic digestion and analyzed by LC-MS/MS. The result of such an experiment is a list of proteins that were co-immunoprecipitated alongside the bait.

Interestingly, our APMS workflow is compatible with label-free quantitative proteomics. Therefore, if needed, we can provide quantitative information on every IPed protein relative to a control condition. This experiment would be ideal to compare the affinity of interaction partners to your protein of interest in two or more conditions.