title: Detection of c-Myc protein-protein interactions and phosphorylation status by immunoprecipitation.
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.
authors.affiliation: Department of Molecular and Medical Genetics, Oregon Health and Science University, Portland, OR, USA.
authors.forename: Colin J
authors.initials: CJ
authors.lastname: Daniel
authors.forename: Xiaoli
authors.initials: X
authors.lastname: Zhang
authors.forename: Rosalie C
authors.initials: RC
authors.lastname: Sears
mesh_terms: D047468:Immunoprecipitation / Q000379:methods*; D010766:Phosphorylation; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D012694:Serine / Q000378:metabolism
chemical_list: D016271:Proto-Oncogene Proteins c-myc; D012694:Serine