The Stat proteins function both as cytoplasmic signal transducers and as activators of transcription. Seven mammalian Stat proteins have been identified: Stat1-4, Stat5a, 5b, and Stat6. Stat3 is a 92kDa protein that is activated as a DNA binding protein through cytokines, such as IL-6, and growth factors, such as EGF. Stat3 is phophorylated at serine 727 (S727) via the MAPK pathway. The S727 residue is located at a conserved Pro-X-Ser-Pro sequence, which is recognized by the protein kinase ERK. Activation through the S727 residue is thought to lead to initiation of transcription. Upon activation, Stat3 dimerizes, translocates to the nucleus, and binds DNA response elements thereby regulating gene expression. It appears that Stat3 binds to DNA as a homodimer, but it is also capable of binding as a heterodimer with Stat1. In addition to serine phosphorylation, Stat3 is also phosphorylated at tyrosine 705 by JAK1 in response to cytokine stimulation. Stat3 is widely expressed and can bind to the sis-inducible element (SIE) site from the c-fos promoter. This site is similar to the GAS element that is present in IFN-g-induced genes. Thus, phosphorylation of S727 in Stat3 occurs in response to growth factors and cytokines, and is essential for normal transcription activity.
Immunofluorescence, Western Blotting
|Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.|
|Human, Mouse, Rat|
|Phosphorylated Human Stat3|
|Store undiluted at -20°C.|
For Research Use Only.
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