Related Experiment Video
Updated: Apr 18, 2026
Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
Published on: January 18, 2020
[Functional analysis of cancer-derived immunoglobulin G whole molecule-interacting proteins identified by LC-MS/MS]
Ju-Ping Wang1, Han-Ying Chen, Hui Peng
1Provincial Key Laboratory of Infectious Diseases and Molecular Immunopathology, Department of Pathology, Shantou University Medical College, Shantou 515041, China.E-mail: wjp0128@aliyun.com.
Objective:
To identify cancer-derived immunoglobulin G (IgG) whole molecule-interacting proteins to provide important clues for studying IgG biological functions.
Methos:
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.
