Lane 1: Hela cell lysate
Lane 2: A431 cell lysate
Lane 1: NIH/3T3 cell lysate
Lane 2: Jurkat cell lysate
Recombinant Rabbit monoclonal primary
Recombinant Phospho STAT3 (S727) Monoclonal Antibody (ET1607-39)
Synthetic phospho-peptide corresponding to residues surrounding ser727 of human stat3.
Hela cell lysate, A431 cell lysate, NIH/3T3 cell lysate, Jurkat cell lysate, Hela, A431, NIH/3T3, rat liver tissue, rat brain tissue, rat kidney tissue, human lung tissue.
Store at +4C after thawing. Aliquot store at -20C . Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
1110034C02Rik antibody; Acute Phase Response Factor antibody; Acute-phase response factor antibody; ADMIO antibody; APRF antibody; AW109958 antibody; DNA binding protein APRF antibody; FLJ20882 antibody; HIES antibody; MGC16063 antibody; Signal transducer and activator of transcription 3 (acute phase response factor) antibody; Signal transducer and activator of transcription 3 antibody; STAT 3 antibody; Stat3 antibody; STAT3_HUMAN antibody
Belongs to the transcription factor STAT family.
Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
Tyrosine phosphorylated upon stimulation with EGF. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity. ARL2BP may participate in keeping the phosphorylated state of STAT3 within the nucleus. Upon LPS challenge, phosphorylated within the nucleus by IRAK1. Upon erythropoietin treatment, phosphorylated on Ser-727 by RPS6KA5. Phosphorylation at Tyr-705 by PTK6 or FER leads to an increase of its transcriptional activity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling.; Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.; Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.; (Microbial infection) Phosphorylated on Tyr-705 in the presence of S.typhimurium SarA.; S-palmitoylated by ZDHHC19 in SH2 putative lipid-binding pockets, leading to homodimerization. Nuclear STAT3 is highly palmitoylated (about 75%) compared with cytoplasmic STAT3 (about 20%).; S-stearoylated, probably by ZDHHC19.
Membrane receptor signaling by various ligands, including interferons and growth hormones such as EGF, induces activation of JAK kinases which then leads to tyrosine phosphorylation of the various Stat transcription factors. Stat1 and Stat2 are induced by IFN-α and form a heterodimer which is part of the ISGF3 transcription factor complex. Although early reports indicate Stat3 activation by EGF and IL-6, it has been shown that Stat3β appears to be activated by both while Stat3α is activated by EGF, but not by IL-6. Highest expression of Stat4 is seen in testis and myeloid cells. IL-12 has been identified as an activator of Stat4. Stat5 has been shown to be activated by Prolactin and by IL-3. Stat6 is involved in IL-4 activated signaling pathways.