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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 immunopreciptitation.

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