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Western blot antibodies are Y-shaped proteins used in the Western blot immunoassay to detect associated proteins in tissue cultures. Monoclonal and polyclonal antibodies can be made from various substances. The process involves gel electrophoresis and “blotting” to identify proteins. Applications include disease diagnosis and forensic science.
Western blot antibodies are large Y-shaped proteins, or immunoglobulins, manufactured for use in the Western blot immunoassay, a test for detecting an associated protein in a tissue culture. Many companies specialize in the manufacture and supply of antibodies to laboratories using the Western blot method. There are two types of Western blot antibodies that can be made in the laboratory: monoclonal and biclonal. The method and type of antibody produced depend on how the antibody reproduces naturally within the host body. During Western blot testing, a process called gel electrophoresis is used to separate the tissue sample’s native proteins from the targeted Western blot antibodies, leading to a positive identification.
Almost any substance can be used to make a monoclonal antibody that will bind to its related protein in a Western blot culture. Polyclonal antibodies are made in much the same way, but the process is more complicated as the antibodies must be harvested from immune B-cell resources instead of simply being cloned from a parent cell. The growing technology of producing immunoglobulins from various substances is considered an invaluable tool in biochemistry, molecular biology and medicine. Western blot analysis can detect proteins associated with HIV, Lyme disease, and Creutzfeldt-Jakob disease, mad cow disease, leading doctors to make a definitive diagnosis earlier in the course of disease progression . In addition to these applications, forensic science can also use Western blot antibody technology to identify blood samples or other substances at the crime scene.
Regardless of its application, the process of identifying a targeted protein in a tissue sample begins with reproducing a quantity of the antibody from a known source. Monoclonal antibodies can be made from existing cultures, but the process of making polyclonal antibodies takes much longer. The process typically involves injecting a host animal, such as a mouse or goat, with inactive or live particulate matter, at which point the animal’s B lymphocytes produce antigen-specific immunoglobulins. Next, detergents and buffers are added to the sample which will prevent the digestion of the immunoglobulins by any native enzymes, and gel electrophoresis is used to separate the proteins by molecular weight or isoelectric charge. Western blot antibodies are now ready to undergo the process of “blotting,” which is the transfer of antibodies to a membrane by noting the specific blot patterns produced during the transfer that are unique to the protein being identified.
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