P-Stat1 (Ser727) (D3B7) R mAb (InTraSeq 3‘ Conjugate 3039)

The Stat1 transcription factor is activated in response to a large number of ligands (1) and is essential for responsiveness to IFN-α and IFN-γ (2,3). Phosphorylation of Stat1 at Tyr701 induces Stat1 dimerization, nuclear translocation, and DNA binding (4). Stat1 protein exists as a pair of isoforms, Stat1α (91 kDa) and the splice variant Stat1β (84 kDa). In most cells, both isoforms are activated by IFN-α, but only Stat1α is activated by IFN-γ. The inappropriate activation of Stat1 occurs in many tumors (5). In addition to tyrosine phosphorylation, Stat1 is also phosphorylated at Ser727 through a p38 mitogen-activated protein kinase (MAPK)-dependent pathway in response to IFN-α and other cellular stresses (6). Serine phosphorylation may be required for the maximal induction of Stat1-mediated gene activation. 1.Heim, M.H. (1999) J Recept Signal Transduct Res 19, 75-120. 2.Durbin, J.E. et al. (1996) Cell 84, 443-50. 3.Meraz, M.A. et al. (1996) Cell 84, 431-42. 4.Ihle, J.N. et al. (1994) Trends Biochem Sci 19, 222-7. 5.Frank, D.A. (1999) Mol Med 5, 432-56. 6.Wen, Z. et al. (1995) Cell 82, 241-50.