Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Signal transducer and activator of transcription 3 (Acute-phase response factor)

 STAT3_MOUSE             Reviewed;         770 AA.
P42227; A2A5D1; B7ZC17;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 201.
RecName: Full=Signal transducer and activator of transcription 3;
AltName: Full=Acute-phase response factor;
Name=Stat3; Synonyms=Aprf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A), AND PROTEIN SEQUENCE OF
154-158; 181-185 AND 632-640.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=7512451; DOI=10.1016/0092-8674(94)90235-6;
Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T.,
Yoshida K., Sudo T., Naruto M., Kishimoto T.;
"Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-
related transcription factor involved in the gp130-mediated signaling
pathway.";
Cell 77:63-71(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DEL-701).
TISSUE=Brain;
PubMed=7523373;
Raz R., Durbin J.E., Levy D.E.;
"Acute phase response factor and additional members of the interferon-
stimulated gene factor 3 family integrate diverse signals from
cytokines, interferons, and growth factors.";
J. Biol. Chem. 269:24391-24395(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
TISSUE=Thymus;
PubMed=8140422; DOI=10.1126/science.8140422;
Zhong Z., Wen Z., Darnell J.E. Jr.;
"Stat3: a STAT family member activated by tyrosine phosphorylation in
response to epidermal growth factor and interleukin-6.";
Science 264:95-98(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3B).
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Liver;
PubMed=7568080; DOI=10.1073/pnas.92.20.9097;
Schaefer T.S., Sanders L.K., Nathans D.;
"Cooperative transcriptional activity of Jun and Stat3 beta, a short
form of Stat3.";
Proc. Natl. Acad. Sci. U.S.A. 92:9097-9101(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM STAT3A).
STRAIN=129/SvJ;
PubMed=11161808; DOI=10.1006/geno.2000.6433;
Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
Oka T., Dewar K., Hennighausen L.;
"Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
zebrafish to mouse.";
Genomics 71:150-155(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
STRAIN=C57BL/6J, and NOD/LtJ;
Davoodi-Semiromi A., She J.-X.;
"A mutant Stat5b with weaker DNA binding defines a key defective
pathway in non-obese diabetic (NOD) mice.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM STAT3A).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION AT SER-727, AND MUTAGENESIS.
PubMed=7543024; DOI=10.1016/0092-8674(95)90311-9;
Wen Z., Zhong Z., Darnell J.E. Jr.;
"Maximal activation of transcription by Stat1 and Stat3 requires both
tyrosine and serine phosphorylation.";
Cell 82:241-250(1995).
[10]
INTERACTION WITH PIAS3.
TISSUE=Thymus;
PubMed=9388184; DOI=10.1126/science.278.5344.1803;
Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.;
"Specific inhibition of Stat3 signal transduction by PIAS3.";
Science 278:1803-1805(1997).
[11]
PHOSPHORYLATION BY FER, AND INTERACTION WITH FER.
PubMed=10878010; DOI=10.1074/jbc.M003402200;
Priel-Halachmi S., Ben-Dor I., Shpungin S., Tennenbaum T.,
Molavani H., Bachrach M., Salzberg S., Nir U.;
"FER kinase activation of Stat3 is determined by the N-terminal
sequence.";
J. Biol. Chem. 275:28902-28910(2000).
[12]
INTERACTION WITH STATIP1.
PubMed=10954736; DOI=10.1073/pnas.170192197;
Collum R.G., Brutsaert S., Lee G., Schindler C.;
"A Stat3-interacting protein (StIP1) regulates cytokine signal
transduction.";
Proc. Natl. Acad. Sci. U.S.A. 97:10120-10125(2000).
[13]
PHOSPHORYLATION AT TYR-705 AND SER-727.
PubMed=11553624; DOI=10.1074/jbc.M106044200;
Zhang Y., Liu G., Dong Z.;
"MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated
mouse epidermal JB6 cells.";
J. Biol. Chem. 276:42534-42542(2001).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-705.
PubMed=11294897; DOI=10.1091/mbc.12.4.931;
Hart K.C., Robertson S.C., Donoghue D.J.;
"Identification of tyrosine residues in constitutively activated
fibroblast growth factor receptor 3 involved in mitogenesis, Stat
activation, and phosphatidylinositol 3-kinase activation.";
Mol. Biol. Cell 12:931-942(2001).
[15]
FUNCTION.
PubMed=12594516; DOI=10.1038/nature01388;
Bates S.H., Stearns W.H., Dundon T.A., Schubert M., Tso A.W., Wang Y.,
Banks A.S., Lavery H.J., Haq A.K., Maratos-Flier E., Neel B.G.,
Schwartz M.W., Myers M.G. Jr.;
"STAT3 signalling is required for leptin regulation of energy balance
but not reproduction.";
Nature 421:856-859(2003).
[16]
INTERACTION WITH NLK, PHOSPHORYLATION AT SER-727, AND MUTAGENESIS OF
SER-727.
PubMed=15004007; DOI=10.1101/gad.1166904;
Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N.,
Matsumoto K., Shibuya H.;
"Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm
induction.";
Genes Dev. 18:381-386(2004).
[17]
SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-77; LEU-78; PHE-174; ARG-609
AND TYR-705, INTERACTION WITH KPNA4 AND KPNA5, AND NUCLEAR IMPORT
MOTIF.
PubMed=15919823; DOI=10.1073/pnas.0501643102;
Liu L., McBride K.M., Reich N.C.;
"STAT3 nuclear import is independent of tyrosine phosphorylation and
mediated by importin-alpha3.";
Proc. Natl. Acad. Sci. U.S.A. 102:8150-8155(2005).
[18]
INTERACTION WITH SIPAR.
STRAIN=Swiss Webster / NIH;
Ning H., Rong Y., Zhang Y., Chang Z.;
"SIPAR interacts with STAT3 to regulate its signal pathway.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 32:173-179(2005).
[19]
FUNCTION, AND PHOSPHORYLATION.
PubMed=16825198; DOI=10.1074/jbc.M601991200;
Gonzalez R.R., Cherfils S., Escobar M., Yoo J.H., Carino C.,
Styer A.K., Sullivan B.T., Sakamoto H., Olawaiye A., Serikawa T.,
Lynch M.P., Rueda B.R.;
"Leptin signaling promotes the growth of mammary tumors and increases
the expression of vascular endothelial growth factor (VEGF) and its
receptor type two (VEGF-R2).";
J. Biol. Chem. 281:26320-26328(2006).
[20]
INTERACTION WITH STMN3.
PubMed=16401721; DOI=10.1083/jcb.200503021;
Ng D.C., Lin B.H., Lim C.P., Huang G., Zhang T., Poli V., Cao X.;
"Stat3 regulates microtubules by antagonizing the depolymerization
activity of stathmin.";
J. Cell Biol. 172:245-257(2006).
[21]
INTERACTION WITH ARL2BP.
PubMed=18234692; DOI=10.1093/intimm/dxm154;
Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
Matsuda T.;
"BART is essential for nuclear retention of STAT3.";
Int. Immunol. 20:395-403(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-714 AND SER-727, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[24]
PHOSPHORYLATION AT SER-727, AND INTERACTION WITH NEK6.
PubMed=20595392; DOI=10.1074/jbc.M110.137190;
Jeon Y.J., Lee K.Y., Cho Y.Y., Pugliese A., Kim H.G., Jeong C.H.,
Bode A.M., Dong Z.;
"Role of NEK6 in tumor promoter-induced transformation in JB6 C141
mouse skin epidermal cells.";
J. Biol. Chem. 285:28126-28133(2010).
[25]
PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
[26]
FUNCTION.
PubMed=23084476; DOI=10.1016/j.molcel.2012.09.013;
Shen S., Niso-Santano M., Adjemian S., Takehara T., Malik S.A.,
Minoux H., Souquere S., Marino G., Lachkar S., Senovilla L.,
Galluzzi L., Kepp O., Pierron G., Maiuri M.C., Hikita H., Kroemer R.,
Kroemer G.;
"Cytoplasmic STAT3 represses autophagy by inhibiting PKR activity.";
Mol. Cell 48:667-680(2012).
[27]
INTERACTION WITH OCAD1, AND SUBUNIT.
PubMed=23972987; DOI=10.1016/j.celrep.2013.07.029;
Sinha A., Khadilkar R.J., Vinay K.S., Roychowdhury Sinha A.,
Inamdar M.S.;
"Conserved regulation of the Jak/STAT pathway by the endosomal protein
asrij maintains stem cell potency.";
Cell Rep. 4:649-658(2013).
[28]
FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
PubMed=23401489; DOI=10.1084/jem.20120260;
Choi S.M., McAleer J.P., Zheng M., Pociask D.A., Kaplan M.H., Qin S.,
Reinhart T.A., Kolls J.K.;
"Innate Stat3-mediated induction of the antimicrobial protein
Reg3gamma is required for host defense against MRSA pneumonia.";
J. Exp. Med. 210:551-561(2013).
[29]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 136-716.
PubMed=9671298; DOI=10.1038/28101;
Becker S., Groner B., Mueller C.W.;
"Three-dimensional structure of the Stat3beta homodimer bound to
DNA.";
Nature 394:145-151(1998).
[30]
DISRUPTION PHENOTYPE.
PubMed=9108058;
Takeda K., Noguchi K., Shi W., Tanaka T., Matsumoto M., Yoshida N.,
Kishimoto T., Akira S.;
"Targeted disruption of the mouse Stat3 gene leads to early embryonic
lethality.";
Proc. Natl. Acad. Sci. U.S.A. 94:3801-3804(1997).
[31]
FUNCTION.
PubMed=20215569; DOI=10.1210/en.2009-1199;
Kostromina E., Gustavsson N., Wang X., Lim C.Y., Radda G.K., Li C.,
Han W.;
"Glucose intolerance and impaired insulin secretion in pancreas-
specific signal transducer and activator of transcription-3 knockout
mice are associated with microvascular alterations in the pancreas.";
Endocrinology 151:2050-2059(2010).
-!- FUNCTION: Signal transducer and transcription activator that
mediates cellular responses to interleukins, KITLG/SCF, LEP and
other growth factors. Once activated, recruits coactivators, such
as NCOA1 or MED1, to the promoter region of the target gene. May
mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and
FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements
identified in the promoters of various acute-phase protein genes.
Activated by IL31 through IL31RA. Acts as a regulator of
inflammatory response by regulating differentiation of naive
CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg):
deacetylation and oxidation of lysine residues by LOXL3, leads to
disrupt STAT3 dimerization and inhibit its transcription activity
(By similarity). Involved in cell cycle regulation by inducing the
expression of key genes for the progression from G1 to S phase,
such as CCND1 (By similarity). Mediates the effects of LEP on
melanocortin production, body energy homeostasis and lactation
(PubMed:12594516). May play an apoptotic role by transctivating
BIRC5 expression under LEP activation (PubMed:16825198).
Cytoplasmic STAT3 represses macroautophagy by inhibiting
EIF2AK2/PKR activity (By similarity). Plays a crucial role in
basal beta cell functions, such as regulation of insulin secretion
(PubMed:20215569). Plays an important role in host defense in
methicillin-resistant S.aureus lung infection by regulating the
expression of the antimicrobial lectin REG3G (PubMed:23401489).
{ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:11294897,
ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:16825198,
ECO:0000269|PubMed:20215569, ECO:0000269|PubMed:23084476,
ECO:0000269|PubMed:23401489}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1,
SIPAR, SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence
of IL23. Interacts (via SH2 domain) with NLK. Interacts with
ARL2BP; the interaction is enhanced by LIF and JAK1 expression (By
similarity). Interacts with KPNA4 and KPNA5; KPNA4 may be the
primary mediator of nuclear import (By similarity). Interacts with
CAV2; the interaction is increased on insulin-induced tyrosine
phosphorylation of CAV2 and leads to STAT3 activation (By
similarity). Interacts with ARL2BP; interaction is enhanced with
ARL2. Interacts with NEK6 (By similarity). Binds to CDK9 when
activated and nuclear. Interacts with BMX. Interacts with
ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on
stimulation by IL6, CNTF or OSM and inhibits the DNA binding
activity of STAT3. In prostate cancer cells, interacts with STAT3
and promotes DNA binding activity of STAT3. Interacts with STMN3,
antagonizing its microtubule-destabilizing activity. Interacts
with the 'Lys-129' acetylated form of BIRC5/survivin. Interacts
with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the
kinase catalytic domain) (By similarity). Interacts with FGFR4 (By
similarity). Interacts with STAT3; the interaction is independent
of STAT3 TYR-705 phosphorylation status (By similarity). Interacts
with OCAD1 (PubMed:23972987). {ECO:0000250|UniProtKB:P40763,
ECO:0000250|UniProtKB:P52631, ECO:0000269|PubMed:10878010,
ECO:0000269|PubMed:10954736, ECO:0000269|PubMed:11553624,
ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15919823,
ECO:0000269|PubMed:16401721, ECO:0000269|PubMed:18234692,
ECO:0000269|PubMed:20595392, ECO:0000269|PubMed:23972987,
ECO:0000269|PubMed:9388184, ECO:0000269|Ref.18}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-602878, EBI-602878;
Q80VH0:Bank1; NbExp=4; IntAct=EBI-602878, EBI-646949;
Q64261:Cdk6; NbExp=3; IntAct=EBI-602878, EBI-847380;
O54784:Dapk3; NbExp=8; IntAct=EBI-602878, EBI-77359;
P30084:ECHS1 (xeno); NbExp=3; IntAct=EBI-602878, EBI-719602;
P70424:Erbb2; NbExp=4; IntAct=EBI-602878, EBI-2945468;
Q8TAE8:GADD45GIP1 (xeno); NbExp=3; IntAct=EBI-602878, EBI-372506;
O35387:Hax1; NbExp=11; IntAct=EBI-602878, EBI-642449;
P40189:IL6ST (xeno); NbExp=4; IntAct=EBI-602878, EBI-1030834;
Q00175:Pgr; NbExp=4; IntAct=EBI-602878, EBI-346821;
Q9NRF2:SH2B1 (xeno); NbExp=5; IntAct=EBI-602878, EBI-310491;
P48025:Syk; NbExp=5; IntAct=EBI-602878, EBI-300116;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
present in the cytoplasm without stimuli. Upon leukemia inhibitory
factor (LIF) stimulation, accumulates in the nucleus. The complex
composed of BART and ARL2 plays an important role in the nuclear
translocation and retention of STAT3 (By similarity). Shuttles
between the nucleus and the cytoplasm. Translocated into the
nucleus upon tyrosine phosphorylation and dimerization, in
response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4.
Constitutive nuclear presence is independent of tyrosine
phosphorylation. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Stat3A;
IsoId=P42227-1; Sequence=Displayed;
Name=Stat3B;
IsoId=P42227-2; Sequence=VSP_006287;
Name=Del-701;
IsoId=P42227-3; Sequence=VSP_010475;
-!- TISSUE SPECIFICITY: STAT3A is seen in the liver, spleen, and
kidney. STAT3B is also detected in the liver, although in a much
less abundant manner. Expressed in the lung and an increase in
expression levels seen during methicillin-resistant S.aureus
infection. {ECO:0000269|PubMed:23401489}.
-!- PTM: Activated through tyrosine phosphorylation by BMX. Tyrosine
phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF,
CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes
phosphorylation on tyrosine residues and subsequent translocation
to the nucleus. Tyrosine phosphorylated in response to
constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4.
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. Tyrosine phosphorylated upon stimulation
with EGF. Upon LPS challenge, phosphorylated within the nucleus by
IRAK1 (By similarity). Upon UV-A treatment, phosphorylated on Ser-
727 by RPS6KA5 (By similarity). Dephosphorylation on tyrosine
residues by PTPN2 negatively regulates IL6/interleukin-6 signaling
(By similarity). Phosphorylation at Tyr-705 by FER or PTK6 leads
to an increase of its transcriptional activity.
{ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:10878010,
ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11553624,
ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:16825198,
ECO:0000269|PubMed:20595392, ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:23401489, ECO:0000269|PubMed:7543024}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P40763}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P40763}.
-!- DISRUPTION PHENOTYPE: Early embryonic lethality, day 6.5-7.5.
Conditional, tissue specific mutants are variably viable and show
diverse defects including obesity, diabetes, thermal dysregulation
and infertility. {ECO:0000269|PubMed:20215569,
ECO:0000269|PubMed:9108058}.
-!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L29278; AAA37254.1; -; mRNA.
EMBL; U08378; AAA56668.1; -; mRNA.
EMBL; U06922; AAA19452.1; -; mRNA.
EMBL; U30709; AAC52612.1; -; mRNA.
EMBL; AF246978; AAL59017.1; -; Genomic_DNA.
EMBL; AY299489; AAQ75418.1; -; mRNA.
EMBL; AY299490; AAQ75419.1; -; mRNA.
EMBL; AL591466; CAM19461.1; -; Genomic_DNA.
EMBL; AL591466; CAX15620.1; -; Genomic_DNA.
EMBL; BC003806; AAH03806.1; -; mRNA.
CCDS; CCDS25440.1; -. [P42227-1]
CCDS; CCDS25441.1; -. [P42227-2]
CCDS; CCDS48934.1; -. [P42227-3]
PIR; I49508; I49508.
RefSeq; NP_998824.1; NM_213659.3. [P42227-1]
RefSeq; NP_998825.1; NM_213660.3. [P42227-3]
UniGene; Mm.249934; -.
UniGene; Mm.473190; -.
PDB; 1BG1; X-ray; 2.25 A; A=127-723.
PDB; 3CWG; X-ray; 3.05 A; A/B=127-688.
PDB; 4E68; X-ray; 2.58 A; A=127-723.
PDB; 4ZIA; X-ray; 2.70 A; A/B/C/D/E=3-127.
PDBsum; 1BG1; -.
PDBsum; 3CWG; -.
PDBsum; 4E68; -.
PDBsum; 4ZIA; -.
ProteinModelPortal; P42227; -.
SMR; P42227; -.
BioGrid; 203523; 23.
CORUM; P42227; -.
DIP; DIP-442N; -.
IntAct; P42227; 32.
MINT; MINT-4135802; -.
STRING; 10090.ENSMUSP00000120152; -.
BindingDB; P42227; -.
ChEMBL; CHEMBL5402; -.
MoonProt; P42227; -.
iPTMnet; P42227; -.
PhosphoSitePlus; P42227; -.
EPD; P42227; -.
MaxQB; P42227; -.
PaxDb; P42227; -.
PeptideAtlas; P42227; -.
PRIDE; P42227; -.
Ensembl; ENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040. [P42227-3]
Ensembl; ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040. [P42227-2]
Ensembl; ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040. [P42227-1]
GeneID; 20848; -.
KEGG; mmu:20848; -.
UCSC; uc007lmp.1; mouse. [P42227-1]
UCSC; uc007lmq.1; mouse. [P42227-3]
CTD; 6774; -.
MGI; MGI:103038; Stat3.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOGENOM; HOG000220792; -.
HOVERGEN; HBG055669; -.
InParanoid; P42227; -.
KO; K04692; -.
OMA; NSMSFAE; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P42227; -.
TreeFam; TF318648; -.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-447115; Interleukin-12 family signaling.
Reactome; R-MMU-6783589; Interleukin-6 family signaling.
Reactome; R-MMU-6783783; Interleukin-10 signaling.
Reactome; R-MMU-6785807; Interleukin-4 and 13 signaling.
Reactome; R-MMU-8849474; PTK6 Activates STAT3.
Reactome; R-MMU-8854691; Interleukin-20 family signaling.
Reactome; R-MMU-8875791; MET activates STAT3.
Reactome; R-MMU-8983432; Interleukin-15 signaling.
Reactome; R-MMU-8984722; Interleukin-35 Signalling.
ChiTaRS; Stat3; mouse.
EvolutionaryTrace; P42227; -.
PRO; PR:P42227; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000004040; -.
ExpressionAtlas; P42227; baseline and differential.
Genevisible; P42227; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
GO; GO:0031730; F:CCR5 chemokine receptor binding; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048708; P:astrocyte differentiation; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI.
GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0042755; P:eating behavior; IMP:MGI.
GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
GO; GO:0001754; P:eye photoreceptor cell differentiation; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:MGI.
GO; GO:0007259; P:JAK-STAT cascade; TAS:UniProtKB.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; IDA:BHF-UCL.
GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; ISO:MGI.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0045820; P:negative regulation of glycolytic process; IMP:MGI.
GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:2001223; P:negative regulation of neuron migration; IGI:MGI.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI.
GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISO:MGI.
GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; IEA:Ensembl.
GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; TAS:Reactome.
GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
GO; GO:0060019; P:radial glial cell differentiation; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; IMP:UniProtKB.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; ISO:MGI.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0044321; P:response to leptin; IDA:UniProtKB.
GO; GO:0019953; P:sexual reproduction; IMP:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; IMP:UniProtKB.
GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:MGI.
CDD; cd10374; SH2_STAT3; 1.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR035855; STAT3_SH2.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_N.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Acute phase;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; SH2 domain; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P40763}.
CHAIN 2 770 Signal transducer and activator of
transcription 3.
/FTId=PRO_0000182418.
DOMAIN 580 670 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOTIF 150 162 Essential for nuclear import.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 601 601 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 601 601 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 615 615 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 615 615 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 631 631 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 631 631 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 685 685 Allysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 685 685 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 705 705 Phosphotyrosine; by FER and PTK6.
{ECO:0000244|PubMed:18034455,
ECO:0000269|PubMed:11294897,
ECO:0000269|PubMed:11553624}.
MOD_RES 707 707 N6-acetyllysine.
{ECO:0000250|UniProtKB:P40763}.
MOD_RES 714 714 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 727 727 Phosphoserine; by DYRK2, NLK, NEK6,
IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE.
{ECO:0000244|PubMed:21183079,
ECO:0000305|PubMed:11553624,
ECO:0000305|PubMed:15004007,
ECO:0000305|PubMed:20595392,
ECO:0000305|PubMed:7543024}.
VAR_SEQ 701 701 Missing (in isoform Del-701).
{ECO:0000303|PubMed:7523373}.
/FTId=VSP_010475.
VAR_SEQ 716 770 TTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLT
FDMDLTSECATSPM -> FIDAVWK (in isoform
Stat3B). {ECO:0000303|PubMed:7568080}.
/FTId=VSP_006287.
MUTAGEN 77 77 V->A: No effect on nuclear import; when
associated with A-78 and W-174.
{ECO:0000269|PubMed:15919823}.
MUTAGEN 78 78 L->A: No effect on nuclear import; when
associated with A-77 and W-174.
{ECO:0000269|PubMed:15919823}.
MUTAGEN 174 174 F->W: No effect on nuclear import; when
associated with A-77 and A-78.
{ECO:0000269|PubMed:15919823}.
MUTAGEN 609 609 R->A: Nuclear localization to the same
extent as wild-type; when associated with
F-705. {ECO:0000269|PubMed:15919823}.
MUTAGEN 705 705 Y->F: Nuclear localization to the same
extent as wild-type; when associated with
A-609. {ECO:0000269|PubMed:15919823}.
MUTAGEN 727 727 S->A: Decreased transcriptional
activation.
{ECO:0000269|PubMed:15004007}.
CONFLICT 16 16 E -> K (in Ref. 2; AAA19452).
{ECO:0000305}.
CONFLICT 25 25 S -> T (in Ref. 2; AAA19452 and 4;
AAC52612). {ECO:0000305}.
CONFLICT 394 394 M -> I (in Ref. 1; AAA37254).
{ECO:0000305}.
HELIX 3 8 {ECO:0000244|PDB:4ZIA}.
TURN 12 14 {ECO:0000244|PDB:4ZIA}.
HELIX 15 20 {ECO:0000244|PDB:4ZIA}.
STRAND 24 26 {ECO:0000244|PDB:4ZIA}.
HELIX 28 33 {ECO:0000244|PDB:4ZIA}.
HELIX 35 40 {ECO:0000244|PDB:4ZIA}.
HELIX 43 46 {ECO:0000244|PDB:4ZIA}.
HELIX 50 73 {ECO:0000244|PDB:4ZIA}.
HELIX 77 94 {ECO:0000244|PDB:4ZIA}.
HELIX 98 120 {ECO:0000244|PDB:4ZIA}.
HELIX 139 180 {ECO:0000244|PDB:1BG1}.
HELIX 199 237 {ECO:0000244|PDB:1BG1}.
HELIX 239 251 {ECO:0000244|PDB:1BG1}.
HELIX 261 290 {ECO:0000244|PDB:1BG1}.
TURN 297 301 {ECO:0000244|PDB:1BG1}.
HELIX 302 320 {ECO:0000244|PDB:1BG1}.
STRAND 321 328 {ECO:0000244|PDB:1BG1}.
STRAND 338 340 {ECO:0000244|PDB:1BG1}.
STRAND 345 353 {ECO:0000244|PDB:1BG1}.
HELIX 356 358 {ECO:0000244|PDB:1BG1}.
TURN 359 361 {ECO:0000244|PDB:1BG1}.
STRAND 363 369 {ECO:0000244|PDB:1BG1}.
HELIX 371 373 {ECO:0000244|PDB:1BG1}.
STRAND 375 377 {ECO:0000244|PDB:1BG1}.
STRAND 384 388 {ECO:0000244|PDB:1BG1}.
STRAND 391 393 {ECO:0000244|PDB:1BG1}.
HELIX 400 402 {ECO:0000244|PDB:4E68}.
STRAND 404 415 {ECO:0000244|PDB:1BG1}.
STRAND 418 420 {ECO:0000244|PDB:1BG1}.
HELIX 426 428 {ECO:0000244|PDB:1BG1}.
HELIX 432 434 {ECO:0000244|PDB:1BG1}.
STRAND 439 447 {ECO:0000244|PDB:1BG1}.
STRAND 450 457 {ECO:0000244|PDB:1BG1}.
STRAND 461 466 {ECO:0000244|PDB:1BG1}.
HELIX 467 469 {ECO:0000244|PDB:1BG1}.
HELIX 470 483 {ECO:0000244|PDB:1BG1}.
HELIX 492 494 {ECO:0000244|PDB:1BG1}.
HELIX 501 515 {ECO:0000244|PDB:1BG1}.
HELIX 522 533 {ECO:0000244|PDB:1BG1}.
HELIX 546 549 {ECO:0000244|PDB:1BG1}.
STRAND 557 559 {ECO:0000244|PDB:4E68}.
HELIX 561 574 {ECO:0000244|PDB:1BG1}.
STRAND 575 577 {ECO:0000244|PDB:3CWG}.
HELIX 578 581 {ECO:0000244|PDB:1BG1}.
HELIX 593 595 {ECO:0000244|PDB:1BG1}.
TURN 596 600 {ECO:0000244|PDB:1BG1}.
STRAND 608 610 {ECO:0000244|PDB:1BG1}.
STRAND 619 621 {ECO:0000244|PDB:1BG1}.
STRAND 626 628 {ECO:0000244|PDB:1BG1}.
HELIX 642 645 {ECO:0000244|PDB:1BG1}.
HELIX 650 653 {ECO:0000244|PDB:1BG1}.
STRAND 664 666 {ECO:0000244|PDB:1BG1}.
STRAND 671 673 {ECO:0000244|PDB:1BG1}.
TURN 674 676 {ECO:0000244|PDB:1BG1}.
TURN 679 683 {ECO:0000244|PDB:1BG1}.
HELIX 684 686 {ECO:0000244|PDB:1BG1}.
SEQUENCE 770 AA; 88054 MW; 6C00626711C8012D CRC64;
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL
LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA
TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK
SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL
ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ
HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY
QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN
GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY
NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS
GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM
DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN
TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDMD LTSECATSPM


Related products :

Catalog number Product name Quantity
20-372-60044 signal transducer and activator of transcription 3 (acute-phase response factor) - Mouse monoclonal anti-human STAT3 antibody; Acute-phase response factor Monoclonal 0.1 mg
10-782-55123 Signal transducer and activator of transcription 3 - Acute-phase response factor N_A 0.2 mg
10-782-55123 Signal transducer and activator of transcription 3 - Acute-phase response factor N_A 0.05 mg
15-288-22759 Signal transducer and activator of transcription 3 - Acute-phase response factor Polyclonal 0.1 mg
15-288-22759 Signal transducer and activator of transcription 3 - Acute-phase response factor Polyclonal 0.05 mg
201-20-5631 STAT3{signal transducer and activator of transcription 3 (acute-phase response factor)}rabbit.pAb 0.2ml
201-20-5630 STAT3{signal transducer and activator of transcription 3 (acute-phase response factor)}rabbit.pAb 0.2ml
E13812291 Signal Transducer and Activator of Transcription 3 (Acute-Phase Response Factor) (STAT3) ELISA Kit 1
GS-2144a signal transducer and activator of transcription 3 (acute-phase response factor) primary antibody, Host: Rabbit 200ul
E1743m ELISA kit Acute-phase response factor,Aprf,Mouse,Mus musculus,Signal transducer and activator of transcription 3,Stat3 96T
E1743m ELISA Acute-phase response factor,Aprf,Mouse,Mus musculus,Signal transducer and activator of transcription 3,Stat3 96T
U1743m CLIA Acute-phase response factor,Aprf,Mouse,Mus musculus,Signal transducer and activator of transcription 3,Stat3 96T
E1743h ELISA Acute-phase response factor,APRF,Homo sapiens,Human,Signal transducer and activator of transcription 3,STAT3 96T
U1743h CLIA Acute-phase response factor,APRF,Homo sapiens,Human,Signal transducer and activator of transcription 3,STAT3 96T
E1743h ELISA kit Acute-phase response factor,APRF,Homo sapiens,Human,Signal transducer and activator of transcription 3,STAT3 96T
CSB-EL022812PI Pig signal transducer and activator of transcription 3 (acute-phase response factor) (STAT3) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL022812RA Rat signal transducer and activator of transcription 3 (acute-phase response factor) (STAT3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
STAT3 STAT3 Gene signal transducer and activator of transcription 3 (acute-phase response factor)
CSB-EL022812CH Chicken signal transducer and activator of transcription 3 (acute-phase response factor) (STAT3) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL022812MO Mouse signal transducer and activator of transcription 3 (acute-phase response factor) (STAT3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL022812BO Bovine signal transducer and activator of transcription 3 (acute-phase response factor) (STAT3) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-PA022812GA01HU Rabbit anti-human signal transducer and activator of transcription 3 (acute-phase response factor) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA022812GA01HU Rabbit anti-human signal transducer and activator of transcription 3 (acute-phase response factor) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
60044 IgG,signal transducer and activator of transcription 3 (acute_phase response factor) 0.1 mg
10-663-45559 STAT3 Transcription Factor Human - Acute-phase response factor N_A 0.01 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur