Anti-phospho-STAT2 (Tyr689) (Signal Transducers and Activators of Transcription 2)

STAT (for signal transducers and activators of transcription) proteins can be selectively phosphorylated on tyrosine residues by Jak family kinases and some receptors with tyrosine kinase activity. The STAT proteins are highly conserved in their amino termini, but have divergent carboxy termini, which are thought to be essential for their selective activity. Seven STAT proteins have been described (STAT1a, STAT1b, STAT2, STAT3, STAT4, STAT5, and STAT6) and range in molecular weight from 84-113kD. Interferon-a promotes phosphorylation of STAT1 and STAT2, which then form heterodimers that interact with the 48kD DNA binding protein ISGF3. This complex moves to the nucleus where it binds to interferon-stimulated response elements and activates transcription of specific genes. In contrast to interferon-a signaling, interferon-g only induces phosphorylation of STAT1a or b. STAT proteins may be involved in the intracellular signaling of many cytokines and growth factors via the activation of gene expression. Applications: Suitable for use in Western Blot and Immunoprecipitation. Other applications have not been tested. Recommended Dilutions: Western Blot: 1:100 detected phosphorylated STAT2 in 10ug of IFN alpha/gamma treated HeLa cell lysate. HeLa cell lysate and IFN alpha/gamma treated HeLa cell lysate probed with S7970-80 (1:100). Proteins were visualized using an IgG (HRP) goat anti-rabbit secondary and a chemiluminescence detection system., Immunoprecipitation: 10ug immunoprecipitates STAT 2, phosphorylated (Tyr689) from IFN alpha HeLa cell lysates, Optimal dilutions to be determined by the researcher. Positive Control: Untreated and IFN alpha/gamma treated HeLa cell lysate. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.