Western blotting (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 to a membrane (typically nitrocellulose or PVDF), where they are probed using antibodies specific to the target protein. The technique allows researchers to identify and quantify the presence of a specific protein within a complex mixture and analyze protein expression levels, post-translational modifications, and protein-protein interactions.
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