For signal transduction research, the emergence of anti-tyrosine phosphorylation antibodies is a significant event. Tyrosine phosphorylation of proteins and enzymes can only be detected by very dangerous and time consuming radioactivity experiments in the absence of anti-tyrosine phosphorylated antibodies. With anti-tyrosine phosphorylation antibodies, phosphorylation signals can be easily detected by Western Blot or other immunological methods. Conventional assays include detection of endogenous or exogenously expressed phosphorylated proteins on Western Blots with anti-tyrosine phosphorylated antibodies. If the content of the target protein is low, the phosphorylated tyrosine protein can be first enriched by immunoprecipitation, and the level of the target protein can be detected. Anti-tyrosine phosphorylation antibodies are also commonly used to detect changes in total tyrosine phosphorylation levels in cells under different treatment conditions, as an important indicator of many cellular biological phenomena.

We all know that if it is necessary to detect the phosphorylation status of a specific site of a target protein, a phosphorylation-specific antibody at a specific site of the protein can be selected. However, because we are usually studying new phosphorylation sites, or the phosphorylated antibodies at specific sites of these proteins are not good enough, we have to prepare phosphorylated antibodies ourselves. If you have prepared phosphorylated antibodies yourself, you know that the preparation of phosphorylated antibodies is more difficult than the preparation of general antibodies, and a lot of valuable time is wasted. Now foreign scientists have found that general-purpose phosphorylated antibodies can be used, and the same test can be achieved by clever design experiments. Take Yuan's article as an example, they need to detect phosphorylation of BCR-ABL, but they do not have specific phosphorylated antibodies. They first used anti-c-ABL antibody and protein G-agarose beads to immunoprecipitate and enrich BCR-ABL protein, which was then identified by Western-Blot and 4G10 universal tyrosine phosphorylation antibody (pan-phosphotyrosine). Level of tyrosine phosphorylation of the BCR-ABL protein. Another group of scientists led by Clemens used the anti-Dock protein antibody to co-precipitate DACK protein, and then used 4G10 tyrosine phosphorylation antibody to detect the tyrosine phosphorylation level of DACK protein and DSH3PX1 protein. The molecular weight of the protein is used to confirm the protein identity of the corresponding phosphorylated band.

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