Western Blotting
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Western blotting (immunoblotting) is a powerful technique used to separate and identify proteins. Proteins are first separated by size through gel electrophoresis and then transferred onto a membrane, commonly nitrocellulose or PVDF, for detection with specific labeled antibodies or antigens.
Because gel electrophoresis typically denatures proteins, only antibodies recognizing the denatured form of an antigen, either monoclonal or polyclonal, can be used for immunoblotting. This method not only allows precise identification of individual proteins but also provides molecular weight information and distinguishes between isoforms or processed protein products.
Once transferred, proteins can be visualized using staining methods and specifically detected via immunodetection, enabling reliable and detailed analysis of protein expression and modifications.
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Accurate protein detection and analysis through precise immunoblotting techniques.
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