STAT3, phosphorylated (Tyr705) (Signal Transducer and Activator of Transcription 3, Acute-phase Response Factor, APRF)

The signal transducer and activator of transcription (STAT) family of transcription factors is composed of seven family members (STATs 1, 2, 3, 4, 5A, 5B and 6) that are involved in many cell processes (apoptosis, anti-apoptosis, cell differentiation and proliferation), depending upon the cell type. STATs are activated by ligand binding to cytokine receptors and other types of receptors, those receptors associating with Janus kinase (JAK) family members that phosphorylate STAT protein, causing it to translocate to the nucleus. In the nucleus, phosphorylated STAT protein binds to DNA and regulates the transcription of particular genes. Phosphorylation on tyrosine 705 by JAK1&2 is essential for STAT3 dimer formation, nuclear translocation and DNA binding activity.\n\nApplications: \nSuitable for use in Western Blot and Flow Cytometry. Other applications not tested.\n\nRecommended Dilutions:\nWestern Blot: 1:1000\nOptimal dilutions to be determined by the researcher.\n\nPositive Control: \n3T3-L1 adipocytes +/- Leukemia Inhibitory Factor (LIF). \n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

S7971-01A

Size

10 Blots

Applications

ELISA, FC, WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat

Form

Supplied as a liquid in Dulbecco

P Type

Pab

Purity

Purified by immunoaffinity chromatography

Isotype

IgG

References

1. Booz, G.W., et al. (2003) Angiotensin II effects on STAT3 phosphorylation in cardiomyocytes: evidence for Erk-dependent Tyr705 dephosphorylation. Basic Res. Cardiol. 98(1):33-38. 2. Booz, G.W., et al. (2002) Cytokine G-protein signaling crosstalk in cardiomyocytes: attenuation of Jak-STAT activation by endothelin-1. Mol. Cell. Biochem. 240(1-2):39-46. 3. Barton, B.E., et al. (2001) IL-6 signaling by STAT3 participates in the change from hyperplasia to neoplasia in NRP-152 and NRP-154 rat prostatic epithelial cells. BMC Cancer 1(1):19. 4. Boeuf, H., et al. (2001) The ribosomal S6 kinases, cAMP-responsive element-binding, and STAT3 proteins are regulated by different leukemia inhibitory factor signaling pathways in mouse embryonic stem cells. J. Biol. Chem. 276(49):46204-46211. 5. Dumler, I., et al. (1999) Urokinase induces activation and formation of Stat4 and Stat1-Stat2 complexes in human vascular smooth muscle cells. J. Biol. Chem. 274(34):24059-24065. 6. Stephens, J.M., et al. (1998) Activation of signal transducers and activators of transcription 1 and 3 by leukemia inhibitory factor, oncostatin-M, and interferon-gamma in adipocytes. J. Biol. Chem. 273(47):31408-31416. 7. Ihle, J.N. (1996) STATs: signal transducers and activators of transcription. Cell 84(3):331-334. 8. Wen, Z. (1995) Maximal activation of transcription by STAT1 and STAT3 requires both tyrosine and serine phosphorylation. Cell 82(2):241-250.

Additional Info

Recognizes human STAT 3, phosphorylated (Tyr705). Species Crossreactivity: mouse and rat