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Molecular & Cellular Proteomics 3:788-795, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Antibodies Immobilized as Arrays to Profile Protein Post-translational Modifications in Mammalian Cells^*

Stanimir S. Ivanov^,, Alicia S. Chung^¶,, Zheng-long Yuan^||, Ying-jie Guan^||, Katherine V. Sachs, Jonathan S. Reichner^|| and Y. Eugene Chin^,¶,||,**

From the Department of Pathology & Laboratory Medicine, Brown University Medical School, Providence, RI 02912; ^¶ Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University Medical School, Providence, RI 02912; ^|| Department of Surgery, Division of Surgical Research, Rhode Island Hospital and Brown University Medical School, Providence, RI 02912

Previously, we demonstrated that antibodies printed on a solid support were able to detect protein-protein interaction in mammalian cells. Here we further developed the antibody array system for detecting proteins with various post-translational modifications in mammalian cells. In this novel approach, immunoprecipitated proteins were labeled with fluorescent dye followed by incubation over antibody arrays. Targeted proteins, captured by the antibodies immobilized on PVDF membrane or glass slide, were detected by means of near infrared fluorescent scanner or fluorescent microscopy. To demonstrate the application of the antibody arrays in protein post-translational modifications, we profiled protein tyrosine phosphorylation, ubiquitination, and acetylation in mammalian cells under different conditions. Our results indicate that antibody array technology can provide a powerful means of profiling a large number of proteins with different post-translational modifications in cells.

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