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The Stat proteins function as both cytoplasmic signal transducers and activators of transcription. The Stat91/84 (the two proteins are the result of alternate splicing-Stat91 has an additional 38 C-terminal amino acids) and Stat113 were the first identified members of this protein family. These three polypeptides contain both SH2 and SH3 domains and have also been described as members of the ISGF3 (interferon-stimulated gene factor 3) complex. With the discovery of additional members of the Stat family (Stats3 & 4), the nomenclature has been revised to indicate the Stat family members in the order of their discovery. Stat 91, 84, and 113 have become Stat1α, Stat1β, and Stat2, respectively. Stat1α is present in a higher concentration than Stat1β in most cell types. In response to IFNα treatment, Stat1α, Stat1β, and Stat2 become tyrosine-phosphorylated and migrate to the nucleus where they join a 48kDa DNA binding protein and subsequently direct the transcription at IFNα responsive elements. In IFN-γ treated cells, Stat1α (but not Stat2) becomes phosphorylated and forms a dimer. It then enters the nucleus and binds to the IFN-γ activated site (GAS) element in order to direct IFN-γ activated transcription.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
