Western blot (Western blot) is a commonly used experimental method in molecular biology, biochemistry and immunogenetics. The principle of immunoblotting experiment is to use the principle that a specific antibody can specifically bind to its antigen protein to color the sample. By analyzing the coloring position and coloring depth, the expression of the specific protein in the analyzed cells or tissues can be obtained. Information about the situation is used to analyze biological detection techniques that detect specific proteins.
Simply speaking, western blotting experiments detect target proteins through the specific binding between antibodies and antigens. This process usually involves separation of protein samples through SDS-PAGE electrophoresis and then transferring the separated proteins from the gel to a solid support (such as PVDF membrane or nitrocellulose membrane). Then use a specific antibody (primary antibody) to bind to the target protein on the transferred membrane, and then use a labeled secondary antibody to bind to the primary antibody. Finally, appropriate substrates are used for chromogenic or luminescent detection of the protein of interest.
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