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Transcription factor AP-1 (AH119) (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (Jun A)

 JUN_MOUSE               Reviewed;         334 AA.
P05627;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 3.
22-NOV-2017, entry version 180.
RecName: Full=Transcription factor AP-1;
AltName: Full=AH119;
AltName: Full=Activator protein 1;
Short=AP1;
AltName: Full=Proto-oncogene c-Jun;
AltName: Full=V-jun avian sarcoma virus 17 oncogene homolog;
Short=Jun A;
Name=Jun;
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].
PubMed=3136397; DOI=10.1038/334535a0;
Ryseck R.-P., Hirai S., Yaniv M., Bravo R.;
"Transcriptional activation of c-jun during the G0/G1 transition in
mouse fibroblasts.";
Nature 334:535-537(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2457172; DOI=10.1038/334629a0;
Lamph W.W., Wamsley P., Sassone-Corsi P., Verma I.M.;
"Induction of proto-oncogene JUN/AP-1 by serum and TPA.";
Nature 334:629-631(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3186736; DOI=10.1073/pnas.85.22.8464;
Ryder K., Nathans D.;
"Induction of protooncogene c-jun by serum growth factors.";
Proc. Natl. Acad. Sci. U.S.A. 85:8464-8467(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
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).
[5]
INTERACTION WITH MYBBP1A.
PubMed=9447996; DOI=10.1128/MCB.18.2.989;
Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A.,
Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A.,
Ishii S., Gonda T.J.;
"Molecular cloning reveals that the p160 Myb-binding protein is a
novel, predominantly nucleolar protein which may play a role in
transactivation by Myb.";
Mol. Cell. Biol. 18:989-1002(1998).
[6]
INTERACTION WITH DSIPI.
PubMed=11397794; DOI=10.1074/jbc.M101522200;
Mittelstadt P.R., Ashwell J.D.;
"Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ.";
J. Biol. Chem. 276:29603-29610(2001).
[7]
INTERACTION WITH HIVEP3, AND FUNCTION.
PubMed=14707112; DOI=10.1084/jem.20030421;
Oukka M., Wein M.N., Glimcher L.H.;
"Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T
cells.";
J. Exp. Med. 199:15-24(2004).
[8]
FUNCTION, AND PHOSPHORYLATION BY HIPK3.
PubMed=17210646; DOI=10.1128/MCB.02253-06;
Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.;
"Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through
homeodomain-interacting protein kinase 3-mediated Jun N-terminal
kinase and c-Jun phosphorylation.";
Mol. Cell. Biol. 27:2027-2036(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-242 AND
SER-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Heart, Kidney, and Lung;
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).
[11]
INTERACTION WITH RNF187.
PubMed=20852630; DOI=10.1038/ncb2098;
Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J.,
Behrens A.;
"Identification of a co-activator that links growth factor signalling
to c-Jun/AP-1 activation.";
Nat. Cell Biol. 12:963-972(2010).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[13]
INTERACTION WITH PRR7.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
-!- FUNCTION: Transcription factor that recognizes and binds to the
enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of
NR5A1 when phosphorylated by HIPK3 leading to increased
steroidogenic gene expression upon cAMP signaling pathway
stimulation. Involved in activated KRAS-mediated transcriptional
activation of USP28 in colorectal cancer (CRC) cells. Binds to the
USP28 promoter in colorectal cancer (CRC) cells (By similarity).
{ECO:0000250|UniProtKB:P05412, ECO:0000269|PubMed:14707112,
ECO:0000269|PubMed:17210646}.
-!- SUBUNIT: Heterodimer with either FOS or BATF3 or ATF7 (By
similarity). The ATF7/JUN heterodimer is essential for ATF7
transactivation activity. Interacts with SP1, SPIB and TCF20.
Interacts with COPS5; the interaction leads indirectly to its
phosphorylation. Component of the SMAD3/SMAD4/JUN/FOS/complex
which forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer
acts synergistically with the JUN/FOS heterodimer to activate
transcription in response to TGF-beta (By similarity). Interacts
(via its basic DNA binding and leucine zipper domains) with SMAD3
(via an N-terminal domain); the interaction is required for TGF-
beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex
(By similarity). Interacts with DSIPI; the interaction inhibits
the binding of active AP1 to its target DNA (PubMed:11397794).
Interacts with HIVEP3 and MYBBP1A (PubMed:9447996,
PubMed:14707112). Interacts with methylated RNF187
(PubMed:20852630). Binds to HIPK3. Interacts (when phosphorylated)
with FBXW7 (By similarity). Interacts with PRR7 (PubMed:27458189).
Found in a complex with PRR7 and FBXW7 (By similarity). Interacts
with PRR7 and FBXW7; the interaction inhibits ubiquitination-
mediated JUN degradation promoting its phosphorylation and
transcriptional activity (By similarity).
{ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P17325,
ECO:0000269|PubMed:11397794, ECO:0000269|PubMed:14707112,
ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:27458189,
ECO:0000269|PubMed:9447996}.
-!- INTERACTION:
Q64261:Cdk6; NbExp=2; IntAct=EBI-764369, EBI-847380;
P03372:ESR1 (xeno); NbExp=6; IntAct=EBI-764369, EBI-78473;
Q91Y86:Mapk8; NbExp=2; IntAct=EBI-764369, EBI-298784;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
-!- PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances
the transcriptional activity. Phosphorylated by HIPK3.
Phosphorylated by DYRK2 at Ser-246; this primes the protein for
subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at
Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its
ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-
89, Thr-93 and Thr-289 thereby promoting JUN-mediated cell
proliferation and transformation. Phosphorylated by PLK3 following
hypoxia or UV irradiation, leading to increase DNA-binding
activity (By similarity). {ECO:0000250|UniProtKB:P05412}.
-!- PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation.
Ubiquitination takes place following phosphorylation, that
promotes interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.
-!- PTM: Acetylated at Lys-271 by EP300.
{ECO:0000250|UniProtKB:P05412}.
-!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
{ECO:0000305}.
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EMBL; X12761; CAA31252.1; -; mRNA.
EMBL; X12740; CAA31236.1; -; mRNA.
EMBL; J04115; AAA37419.1; -; mRNA.
EMBL; BC002081; AAH02081.1; -; mRNA.
EMBL; BC021888; AAH21888.1; -; mRNA.
CCDS; CCDS18364.1; -.
PIR; A31345; TVMSJA.
RefSeq; NP_034721.1; NM_010591.2.
UniGene; Mm.275071; -.
ProteinModelPortal; P05627; -.
SMR; P05627; -.
BioGrid; 200871; 40.
DIP; DIP-1068N; -.
ELM; P05627; -.
IntAct; P05627; 6.
MINT; MINT-209953; -.
STRING; 10090.ENSMUSP00000054270; -.
ChEMBL; CHEMBL5369; -.
iPTMnet; P05627; -.
PhosphoSitePlus; P05627; -.
EPD; P05627; -.
PaxDb; P05627; -.
PeptideAtlas; P05627; -.
PRIDE; P05627; -.
Ensembl; ENSMUST00000107094; ENSMUSP00000102711; ENSMUSG00000052684.
GeneID; 16476; -.
KEGG; mmu:16476; -.
UCSC; uc008tsq.2; mouse.
CTD; 3725; -.
MGI; MGI:96646; Jun.
eggNOG; KOG0837; Eukaryota.
eggNOG; ENOG410XRWH; LUCA.
GeneTree; ENSGT00390000009929; -.
HOGENOM; HOG000006648; -.
HOVERGEN; HBG001722; -.
InParanoid; P05627; -.
KO; K04448; -.
OMA; KDHVAQL; -.
OrthoDB; EOG091G0N0L; -.
PhylomeDB; P05627; -.
TreeFam; TF323952; -.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:P05627; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000052684; -.
CleanEx; MM_JUN; -.
ExpressionAtlas; P05627; baseline and differential.
Genevisible; P05627; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0005719; C:nuclear euchromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0035976; C:transcription factor AP-1 complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0017053; C:transcriptional repressor complex; IPI:MGI.
GO; GO:0035497; F:cAMP response element binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
GO; GO:0071837; F:HMG box domain binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0031103; P:axon regeneration; IMP:MGI.
GO; GO:0009987; P:cellular process; IMP:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0051365; P:cellular response to potassium ion starvation; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
GO; GO:0035026; P:leading edge cell differentiation; IMP:MGI.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; IMP:MGI.
GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; ISO:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
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; ISO:MGI.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IBA:GO_Central.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0042493; P:response to drug; IDA:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
GO; GO:0009314; P:response to radiation; IBA:GO_Central.
GO; GO:0007184; P:SMAD protein import into nucleus; ISO:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR004827; bZIP.
InterPro; IPR015558; C_Jun/v-Jun.
InterPro; IPR005643; JNK.
InterPro; IPR002112; Leuzip_Jun.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR11462:SF8; PTHR11462:SF8; 1.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF03957; Jun; 1.
PRINTS; PR00043; LEUZIPPRJUN.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 334 Transcription factor AP-1.
/FTId=PRO_0000076430.
DOMAIN 255 318 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 255 282 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 283 311 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
SITE 275 275 Necessary for synergistic transcriptional
activity with SMAD3. {ECO:0000250}.
MOD_RES 2 2 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 8 8 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 56 56 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 73 73 Phosphoserine; by MAPK8 and PLK3.
{ECO:0000305|PubMed:17210646}.
MOD_RES 89 89 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 91 91 Phosphothreonine.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 93 93 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 242 242 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 252 252 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 274 274 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 289 289 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CONFLICT 183 183 S -> C (in Ref. 1; CAA31252).
{ECO:0000305}.
SEQUENCE 334 AA; 35944 MW; 2BE0E4025B8B1CA3 CRC64;
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
LHSQNTLPSV TSAAQPVSGA GMVAPAVASV AGAGGGGGYS ASLHSEPPVY ANLSNFNPGA
LSSGGGAPSY GAAGLAFPSQ PQQQQQPPQP PHHLPQQIPV QHPRLQALKE EPQTVPEMPG
ETPPLSPIDM ESQERIKAER KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST
ANMLREQVAQ LKQKVMNHVN SGCQLMLTQQ LQTF


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U1292p CLIA Activator protein 1,AP1,JUN,Pig,Proto-oncogene c-Jun,Sus scrofa,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292r ELISA Activator protein 1,AP1,Jun,Proto-oncogene c-Jun,Rat,Rattus norvegicus,Rjg-9,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292b CLIA Activator protein 1,AP1,Bos taurus,Bovine,JUN,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292b ELISA kit Activator protein 1,AP1,Bos taurus,Bovine,JUN,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292r CLIA Activator protein 1,AP1,Jun,Proto-oncogene c-Jun,Rat,Rattus norvegicus,Rjg-9,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292r ELISA kit Activator protein 1,AP1,Jun,Proto-oncogene c-Jun,Rat,Rattus norvegicus,Rjg-9,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292b ELISA Activator protein 1,AP1,Bos taurus,Bovine,JUN,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292h ELISA Activator protein 1,AP1,Homo sapiens,Human,JUN,p39,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292h ELISA kit Activator protein 1,AP1,Homo sapiens,Human,JUN,p39,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292h CLIA Activator protein 1,AP1,Homo sapiens,Human,JUN,p39,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
18-785-210089 c-Jun (Ab-93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210090 c-Jun (Ab-170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210088 c-Jun (Ab-91) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210089 c-Jun (Ab-93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210093 c-Jun (Ab-239) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg


 

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