Co-Immunoprecipitation is a classical method for studying protein interactions based on the specific interaction between antibodies and antigens. It is an effective method to determine the physiological interaction of two proteins in intact cells.
When the cells are lysed under non-denaturing conditions, many protein-protein interactions within the intact cells are retained. When the protein A is immunoprecipitated with an antibody of protein A pre-cured on argarose beads, protein B bound to protein A in the body can also be precipitated together. The protein B was detected by protein denaturation and the interaction between the two was confirmed.
advantage:
1. A protein that interacts in its natural state.
2. Protein interactions are carried out in a natural state to avoid artificial effects.
3. Isolation yields a natural conformation of the interacting protein.
Disadvantages:
1. Low affinity and transient protein-protein interactions may not be detected.
2. The combination of the two proteins may involve a third party rather than a direct combination.
Predicting possible binding proteins before the experiment is very important to select the antibody to be detected. If the prediction is not accurate, the experiment will not get the result, and the method itself is at risk.
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