The western blot, also known as protein immunoblot, is widely utilized as an analytical technique for the detection of specific proteins in a sample of tissue extract. With its high capacity, high sensitivity, and specificity, Western Blot is the most widely used method for detecting protein properties, such as qualitative and quantitative detection of tissue antigens, quality of peptide molecules, and detection of antibodies or viral antigens.
In short, the technique consists of staining a protein treated by gel electrophoresis with specific antibodies and then transferring the stained protein to the membrane, which provides the researcher with the information that the specific protein in the analyzed cell or tissue will reveal.
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The name Western Blot was given because of its similarity to the Southern Blot method, a previously developed DNA detection technique. It plays an important role in experiments in immunogenetics, molecular biology, and other disciplines in molecular biology.
Three steps were taken during the experiment:
Tissue Preparation: Samples are taken from whole tissue or cell cultures
Gel electrophoresis: The sample protein is separated using gel electrophoresis, which solves the problem of antibody cross-reactivity.
Transfer: The separated proteins are transferred from the inside of the gel to the membrane.
Thousands of antibodies can be used in various Western blots. One of these (both monoclonal and polyclonal) is the anti-CDC25C monoclonal antibody, also known as the mouse anti-human CDC25C monoclonal antibody. These antibodies were produced by mice immunized with the recombinant CDC25C protein.
These antibodies belong to the MPI phosphatase family. This gene was highly conserved during evolution and plays a key role in regulating cell division.