Abstract: Objective To identify cancer-derived immunoglobulin G (IgG) whole molecule-interacting proteins to provide
important clues for studying IgG biological functions. Methods HeLa cell lysate was immunoprecipitated with rabbit
antihuman IgG whole molecule antibody and normal rabbit IgG. The immunocomplex underwent sodium dodecyl sulfate
polyacrylamide gel electrophoresis (SDS-PAGE) and was detected with silver staining. Three prominently enhanced bands
were subjected to protein identification with liquid chromatography-tandem mass spectrometry (LC-MS/MS), and the MS data
were analyzed with Swiss-Prot database. Cancer-derived IgG whole molecule-interacting proteins were screened and
functionally annotated. Results and Conclusion We identified 6 potential cancer-derived IgG whole molecule-interacting
proteins with co-immunoprecipitation combined with LC-MS/MS, which provides valuable clues for studying the function of
cancer-derived IgG.