Western Blot

A western blot (alternately, immunoblot) is 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 (denaturing conditions) (Figure 1) 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. There are now many reagent companies that specialise in providing antibodies (both monoclonal and polyclonal antibodies) against many thousands of different proteins. This has dramatically reduced the time to carry out a blot. Previously large animals (e.g. sheep, goat - lots of serum) had to be immunised with the target protein twice (secondary immune response generates high affinity antibodies). Then either serum could be purified and used (polyclonal antibodies) or B cells could be isolated from the animal and fused in vitro with mouse myeloma cells to generate hybridomas that then provided single-specificity antibodies (monoclonal antibodies). Commercial antibodies are expensive, though the unbound antibody can be reused between experiments. This method is used in the fields of molecular biology, biochemistry, immunogenetics and other molecular biology disciplines.
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Western blot A technique developed in 1979 that is used to confirm ELISA results. HIV antigen is purified by electrophoresis and attached by [more]Western blot - Community and Resources

A technique in molecular biology, used to separate and identify particular proteins. Called a Western blot merely because it has some similarity to a Southern blot (which is named after its inventor, the British biologist M.E. Southern).

Western blott