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In Situ Detection of Protein Complexes and Modifications by Chemical Ligation Proximity Assay
Journal article   Peer reviewed

In Situ Detection of Protein Complexes and Modifications by Chemical Ligation Proximity Assay

Rui Hong, Esteban Roberts, Christopher Bieniarz and Christopher B Rodell
Bioconjugate chemistry, v 27(7), pp 1690-1696
20 Jul 2016
PMID: 27248443

Abstract

HeLa Cells Humans Phosphorylation Protein Multimerization Protein Processing, Post-Translational Protein Structure, Quaternary Proteins - chemistry Proteins - metabolism Ubiquitination
Protein function is often regulated by protein-protein interactions and post-translational modifications. Detection of these important biological phenomena in fixed biological samples could serve as an invaluable tool in biomedical research, drug development, as well as clinical cancer diagnostics and prognostics. We report here a novel methodology which utilizes unique antibody bioconjugates capable of forming proximity induced chemical ligation to enable in situ detection of proximal targets in fixed biological samples. Using this new methodology, we demonstrate in situ visualization of various protein heterodimers/complexes and post-translational modifications such as phosphorylation and ubiquitination. This new method offers high specificity, sensitivity, flexibility, and ease of use. In addition, the assay preserves critical contextual and heterogeneity information on biomarkers in clinically relevant samples.

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Web of Science research areas
Biochemical Research Methods
Biochemistry & Molecular Biology
Chemistry, Multidisciplinary
Chemistry, Organic
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