- Immunoelectrophoresis is a laboratory technique that combines the principles of electrophoresis and immunodiffusion to separate and identify proteins, particularly antigens, in a sample. This method is especially valuable in clinical and research settings for the analysis of complex mixtures of proteins, such as those found in serum. It allows for both the qualitative and semi-quantitative assessment of specific proteins, including immunoglobulins, enzymes, and acute-phase reactants.
- The process begins with electrophoresis, where a mixture of proteins is placed in a gel matrix, typically agarose, and subjected to an electric field. This causes the proteins to migrate through the gel at different rates depending on their size, shape, and net charge. After separation, a trough is cut parallel to the migration path, and specific antibodies are added. These antibodies diffuse laterally into the gel, and where they meet their corresponding antigens, they form visible precipitin lines. These lines indicate the presence and identity of specific proteins based on antigen-antibody interactions.
- There are several variations of immunoelectrophoresis, such as rocket immunoelectrophoresis and crossed immunoelectrophoresis, which offer different advantages. For instance, rocket immunoelectrophoresis is used for quantifying proteins, while crossed immunoelectrophoresis allows for more precise characterization of antigen mixtures. These techniques are widely applied in immunology, clinical diagnostics, and biomedical research for detecting immunodeficiencies, paraproteinemias, and autoimmune disorders.
- Overall, immunoelectrophoresis remains a fundamental tool for the specific detection and characterization of proteins, offering insights into the immune status and protein profile of biological samples. Despite the development of more advanced methods like ELISA and Western blotting, it continues to be useful due to its clarity, reliability, and ability to analyze multiple proteins simultaneously.
