Western blot analysis (also called immunoblotting) is a widely used analytical technique in molecular biology and immunology to detect specific proteins in a sample of tissue homogenate or extract. It uses gel electrophoresis to separate native or denatured proteins by 3-D structure or by the length of the polypeptide, followed by transfer (blotting) of the separated proteins to a membrane (typically nitrocellulose or PVDF), where they are then 'probed' with antibodies specific to the target protein. The antibody binding is then detected through various methods, such as chemiluminescence or fluorescence, allowing for the identification and quantification of the target protein.
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