What is the difference between western blotting and immunoprecipitation?

Immunoprecipitation involves using antibodies and agarose beads to isolate a target protein from a solution, while western blotting (also known as immunoblotting) uses gel electrophoresis and an antibody probe to analyze proteins.

Immunoprecipitation is useful for working with proteins in their native conformation; however, proteins in immunoprecipitation usually need to be radiolabeled. On the other hand, immunoblotting does not require proteins to be radiolabeled and is also more helpful for determining the amount and sizes of proteins, but requires a higher concentration of antigens than what is needed in immunoprecipitation.