Phospho-Stat1 (Tyr701) antibody detects endogenous levels of Stat1 only when phosphorylated at Tyr701. This antibody detects phosphorylated tyrosine 701 of p91 Stat1 and also the p85 splice variant. It does not appreciably cross-react with the corresponding phosphorylated tyrosine of other Stat proteins. Stat1 antibody detects endogenous levels of total Stat1 α (91kDa) and Stat1 β (84kDa) protein.
Source / Purification
Antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr701 of human Stat1 (Phospho-Stat1 (Tyr701) antibody), or with a synthetic peptide corresponding to a sequence of human Stat1 (Stat1 antibody). Antibodies are purified by protein A and peptide affinity chromatography.
Background
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.