<unk>  using an antibody that recognizes proteins modified with lipoic acid The<unk>  (sometimes called the protein immunoblot), or<unk> ting, is a widely used analytical technique in molecular biology and immunogenetics to detect specific proteins in a sample of tissue homogenate or extract.<unk>  technique uses three elements to achieve its task of separating a specific protein from a complex: separation by size, transfer of protein to a solid support, and marking target protein using a primary and secondary antibody to visualize. A synthetic or animal-derived antibody (known as the primary antibody) is created that recognizes and binds to a specific target protein. The electrophoresis membrane is washed in a solution containing the primary antibody, before excess antibody is washed off. A secondary antibody is added which recognizes and binds to the primary antibody. The secondary antibody is visualized through various methods such as staining, immunofluorescence, and radioactivity, allowing indirect detection of the specific target protein. Other related techniques include dot<unk>  analysis, quantitative dot<unk> , immunohistochemistry and immunocytochemistry, where antibodies are used to detect proteins in tissues and cells by immunostaining, and enzyme-linked immunosorbent assay (ELISA). The name<unk>  is a play on the Southern<unk> , a technique for DNA detection named after its inventor, English biologist Edwin Southern. Similarly, detection of RNA is termed as northern<unk> . The term<unk> " was given by W. Neal Burnette in 1981, although the method itself originated in 1979 in the laboratory of Harry Towbin at the Friedrich Miescher Institute in Basel, Switzerland. Between 1979 and 2019 "it has been mentioned in the titles, abstracts, and keywords of more than 400,000 PubMed-listed publications" and may still be the most used protein-analytical technique.
Western blot
Immunolabeling
Immunoassay
MALDI imaging
Ink blot test
Magnetic immunoassay
Radioimmunoassay
Immunostaining