Phospho-Stat3 (Tyr705) Antibody detects endogenous levels of Stat3 only when phosphorylated at tyrosine 705. The antibody does not cross-react with other Stat proteins when phosphorylated on the corresponding tyrosine residue, but does cross-react with EGFR. Stat3 antibody detects endogenous levels of total Stat3 protein.
Source / Purification
Polyclonal antibodies to Phospho-Stat3 are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr705 of mouse Stat3 (Phospho-Stat3 (Tyr705) Antibody), or with a synthetic peptide corresponding to mouse Stat3 (Stat3 antibody). Antibodies are purified by protein A and peptide affinity chromatography.
Background
The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).