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- W1519016390 abstract "Publisher Summary Transferring materials out of sodium dodecyl sulfate (SDS) gels (blotting) onto a nitrocellulose membrane has become a widely used technique. It not only takes the advantage of the high resolving power of polyacrylamide gel electrophoresis but also allows ready access to the blotted target material by a variety of interaction probes. It is now generally called a Western blot, if the blotted protein is probed or detected with an antibody, and a Southwestern blot, if it is probed with a labeled deoxyribonucleic acid (DNA). More recently a technique called a far-Western blot (or sometimes a west-Western) has gained an increasing use. In a far-Western blot, instead of probing with an antibody, the probing is performed with another protein, taking advantage of specific protein–protein interactions. This approach requires that at least some region (the interaction domain) of a fraction of the blotted target protein be able to refold on the membrane and form a three-dimensional structure containing the interaction site. This approach is particularly useful in determining which subunit of a multisubunit complex is involved in an interaction with the probe protein. This chapter describes methods for determining interaction domains along a polypeptide chain by the ordered fragment ladder far-Western analysis." @default.
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- W1519016390 date "2000-01-01" @default.
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- W1519016390 title "[11] Mapping protein-protein interaction domains using ordered fragment ladder far-Western analysis of hexahistidine-tagged fusion proteins" @default.
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- W1519016390 doi "https://doi.org/10.1016/s0076-6879(00)28396-1" @default.
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