immunofixatie

Immunofixation is a laboratory technique used to identify and characterize specific proteins in a biological sample. It is a variation of electrophoresis that combines the separation power of electrophoresis with the high specificity of immunological reactions. The process begins by separating proteins in a sample, such as serum or urine, based on their electrical charge and size using gel electrophoresis. After the proteins have migrated through the gel matrix, antiserum containing antibodies specific to the proteins of interest is applied directly onto the surface of the gel. These antibodies will then bind to their corresponding target proteins, forming antigen-antibody complexes. These complexes are larger and less mobile than the unbound proteins. After incubation, the unbound proteins are washed away, leaving only the antigen-antibody complexes precipitated in the gel. These precipitated bands are then visualized, typically by staining, allowing for the identification and quantification of the specific proteins present. Immunofixation is particularly useful in diagnosing and monitoring conditions involving abnormal or excessive production of specific proteins, such as multiple myeloma, where it can detect and quantify monoclonal immunoglobulins. It is also employed in the analysis of other body fluids and in research settings for protein identification and purity assessment. The technique offers high sensitivity and specificity for detecting even small amounts of target proteins.