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Submitted on December 4, 2003
Revised on April 29, 2004
Accepted on May 3, 2004

Antibodies immobilized as arrays to profile protein post-translational modifications in mammalian cells

Stanimir S. Ivanov, Alicia S. Chung, Paul Z. Yuan, Angie Y. Guan, Katherine V. Sachs, Jonathan S. Reichner, and Y. Eugene Chin

Pathology & Laboratory Medicine and Surgery Sci, Brown University, Providence, Rhode Island 02903

Corresponding Author: y_eugene_chin{at}brown.edu

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, immuno-precipitated proteins were labeled with fluorescent dye followed by incubation over antibody arrays. Targeted proteins, captured by the antibodies immobilized on polyvinylidene fluoride (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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