Coimmunoprecipitation assay.
As with most other proteins, clock proteins physically interact with one another. Coimmunoprecipitation (coIP) is the most straightforward technique to study protein-protein interactions in vivo, if antibodies against the proteins of interest are available. To perform coIP, first an antibody against a target protein is coupled to Sepharose beads through protein A or G, then the complexes containing the target protein are immunoprecipitated with the antibody-coupled beads by centrifugation. Protein components in the complexes are visualized by Western blotting using antibodies specific to the different components.
Lee
Choogon
C
Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, USA.
D000818:Animals; D000906:Antibodies; D015153:Blotting, Western / Q000379:methods; D056926:CLOCK Proteins; D002940:Circadian Rhythm; D047468:Immunoprecipitation / Q000379:methods*; D046912:Multiprotein Complexes / Q000302:isolation & purification; D015534:Trans-Activators / Q000276:immunology / Q000302:isolation & purification
D000906:Antibodies; D046912:Multiprotein Complexes; D015534:Trans-Activators; D056926:CLOCK Proteins