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Updated: May 8, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Detection of c-Myc protein-protein interactions and phosphorylation status by immunoprecipitation
Colin J Daniel1, Xiaoli Zhang, Rosalie C Sears
1Department of Molecular and Medical Genetics, Oregon Health and Science University, Portland, OR, USA.
Abstract:
Co-immunoprecipitation is an invaluable technique in evaluating native protein-protein interactions in vitro and in vivo. However, it can be difficult to detect interactions of a very transient nature, particularly interactions with phosphatases and kinases. The evaluation of the phosphorylation status of c-Myc can also be challenging with the current commercially available phosphorylation sensitive antibodies. Here, we describe two protocols: one for the co-immunoprecipitation of endogenous c-Myc to detect protein-protein interactions and second, for the immunoprecipitation of endogenous c-Myc to probe for phosphorylation status.
