Millipore system makes Western blots a breeze

The system cuts to just 30 minutes the time needed for blocking, washing, and antibody incubations, and this will allow researchers to optimise blotting protocols, says the firm. "Typically, researchers lack the time to optimize their blotting protocols​," it added. This time-saving, alongside the ability to optimise immunodetection conditions, should improve the quality of Western blot analyses. The Western blot has become a popular a method to detect a specific protein in a given sample of tissue homogenate or extract. It uses gel electrophoresis to separate native or denatured proteins by the length of the polypeptide or by the 3-D structure of the protein (native/ non-denaturing conditions). The proteins are then transferred to a membrane (typically nitrocellulose or PVDF), where they are probed (detected) using antibodies specific to the target protein. Commercial antibodies can be expensive, though the unbound antibody can be reused between experiments. The SNAP i.d. system is compatible with all membrane types and detection methods, such as chemiluminescence and fluorescence demonstrating a flexibility its rivals do not include. Millipore commented that: "Both sensitivity and specificity are equivalent or higher than standard immunodetection, with no additional reagent consumption required. Antibody solutions can be collected and reused, for even more economical immunodetection​." What's unique about the system is the quality of the Western blot produced - achieved by a vacuum-driven technology and built-in flow distributor that drives reagents through the membrane, ensuring even distribution. Three different sizes of blot holders accommodate up to three blots each, and two blot holders can be run in parallel. Thus, researchers can process up to six blots in parallel, quickly optimise conditions, and greatly increase their protein detection throughput. Immunodetection techniques describe any application in which the antibody: antigen interactions are analysed. Immunodetection depends greatly on the specificity of each antibody for its antigen and the optimisation of assay conditions for detection and analysis. Along with western blots and ELISA tests, the most common techniques used in research lab are immunocytochemistry/immunohistochemistry. Radioimmunoassay (RIA) could also be considered an immunodetection method but has proved unpopular over the years as labs are changing over to ELISA in order to reduce the amount of radioactive materials being used. While an example form of immunodetection is used in such things as pregnancy tests, its main use is in pharmaceuticals, particularly in the laboratory screening of drugs. The test relies on the development of a specific antibody to the drug or compound being screened for. This antibody is then used to detect the drug in a sample which may or may not contain the drug or compound of interest. A major hurdle which needs to be overcome to accomplish immunodetection using this method is the development of an antibody that is specific for each drug. The antibody must be produced with a sufficient titre, a measure of concentration, to efficiently detect the presence of the drug. Additionally, the antibody must have sufficient specificity to react only with the drug of interest so that accurate results may be obtained. While these requirements are normally obtainable, they inherently result in a system with severe limitations. The greatest of these limitations is the detection of the drug after it is no longer biologically active.