Proteins control all biological systems in a cell, and while many proteins perform their functions independently, the vast majority of proteins interact with others to execute a full range of biological activities. Characterizing protein-protein interactions through methods such as co-immunoprecipitation (co-IP), pull-down assays, crosslinking, label transfer, and far-western blot analysis is critical to understanding protein function and the biology of the cell. See Table 1 for a list of recommended methods of analysis based on the varying strength of interaction between the proteins under investigation.
Featured protein-protein interaction categories
A reliable tool for studying protein-protein interactions in vivo, and a valuable complement to gene function analysis and drug discovery studies.
Kits, cloning vectors, and reagents designed for this use in quantitative immunoprecipitation.
Magnetic beads are a suitable solid support for biopanning methods, including phage display.
Analyze stable protein complexes by separation using gel electrophoresis.
One of the most popular techniques used for the identification of protein-protein interactions.
A reliable tool for studying protein-protein interactions in vivo, and a valuable complement to gene function analysis and drug discovery studies.
Table 1. Common methods to analyze the various types of protein interactions
| Method | Protein-protein interactions |
|---|---|
| Co-Immunoprecipitation (co-IP) | Stable or strong |
| Pull-Down Assay | Stable or strong |
| Crosslinking Protein Interaction Analysis | Transient or weak |
| Label Transfer Protein Interaction Analysis | Transient or weak |
| Far-Western Blot Analysis | Moderately stable |
For Research Use Only. Not for use in diagnostic procedures.