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Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)

 MK08_MOUSE              Reviewed;         384 AA.
Q91Y86;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 169.
RecName: Full=Mitogen-activated protein kinase 8;
Short=MAP kinase 8;
Short=MAPK 8;
EC=2.7.11.24;
AltName: Full=Stress-activated protein kinase JNK1;
AltName: Full=c-Jun N-terminal kinase 1;
Name=Mapk8; Synonyms=Jnk1, Prkm8;
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], AND INTERACTION WITH MAPK8IP3.
TISSUE=Brain;
PubMed=10523642; DOI=10.1128/MCB.19.11.7539;
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,
Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein
that functions as a scaffold factor in the JNK signaling pathway.";
Mol. Cell. Biol. 19:7539-7548(1999).
[2]
FUNCTION IN PHOSPHORYLATION OF TP53.
PubMed=9393873; DOI=10.1038/sj.onc.1201401;
Hu M.C., Qiu W.R., Wang Y.P.;
"JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases.";
Oncogene 15:2277-2287(1997).
[3]
REGULATION BY MAP2K4.
TISSUE=Embryonic stem cell;
PubMed=9096336; DOI=10.1073/pnas.94.7.3004;
Yang D., Tournier C., Wysk M., Lu H.-T., Xu J., Davis R.J.,
Flavell R.A.;
"Targeted disruption of the MKK4 gene causes embryonic death,
inhibition of c-Jun NH2-terminal kinase activation, and defects in AP-
1 transcriptional activity.";
Proc. Natl. Acad. Sci. U.S.A. 94:3004-3009(1997).
[4]
REGULATION BY MAP2K7, AND COFACTOR.
PubMed=9207092; DOI=10.1073/pnas.94.14.7337;
Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
"Mitogen-activated protein kinase kinase 7 is an activator of the c-
Jun NH2-terminal kinase.";
Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997).
[5]
FUNCTION, ENZYME REGULATION, AND INDUCTION.
TISSUE=Embryonic stem cell, and T-cell;
PubMed=10811224; DOI=10.1038/35011091;
Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J.,
Flavell R.A.;
"JNK is required for effector T-cell function but not for T-cell
activation.";
Nature 405:91-94(2000).
[6]
FUNCTION IN PHOSPHORYLATION OF JDP2.
PubMed=11602244; DOI=10.1016/S0014-5793(01)02907-6;
Katz S., Heinrich R., Aronheim A.;
"The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-
terminal kinase.";
FEBS Lett. 506:196-200(2001).
[7]
SUBUNIT, AND PHOSPHORYLATION AT THR-183 AND TYR-185.
TISSUE=Hippocampus;
PubMed=11562351; DOI=10.1101/gad.922801;
Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A.,
Rakic P., Davis R.J.;
"Requirement of the JIP1 scaffold protein for stress-induced JNK
activation.";
Genes Dev. 15:2421-2432(2001).
[8]
INTERACTION WITH SPAG9.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[9]
IDENTIFICATION IN A COMPLEX WITH MAPK8IP1 AND ARHGEF28.
PubMed=14499478; DOI=10.1016/S0169-328X(03)00263-8;
Wu J., Zhai J., Lin H., Nie Z., Ge W.-W., Garcia-Bermejo L.,
Muschel R.J., Schlaepfer W.W., Canete-Soler R.;
"Cytoplasmic retention sites in p190RhoGEF confer anti-apoptotic
activity to an EGFP-tagged protein.";
Brain Res. Mol. Brain Res. 117:27-38(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[11]
INTERACTION WITH JAMP.
PubMed=16166642; DOI=10.1128/MCB.25.19.8619-8630.2005;
Kadoya T., Khurana A., Tcherpakov M., Bromberg K.D., Didier C.,
Broday L., Asahara T., Bhoumik A., Ronai Z.;
"JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein,
regulates duration of JNK activity.";
Mol. Cell. Biol. 25:8619-8630(2005).
[12]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=16618812; DOI=10.1083/jcb.200511055;
Tararuk T., Ostman N., Li W., Bjorkblom B., Padzik A., Zdrojewska J.,
Hongisto V., Herdegen T., Konopka W., Courtney M.J., Coffey E.T.;
"JNK1 phosphorylation of SCG10 determines microtubule dynamics and
axodendritic length.";
J. Cell Biol. 173:265-277(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, 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).
[14]
INTERACTION WITH NFE2, AND FUNCTION.
PubMed=19966288; DOI=10.1073/pnas.0909153107;
Lee T.L., Shyu Y.C., Hsu P.H., Chang C.W., Wen S.C., Hsiao W.Y.,
Tsai M.D., Shen C.K.;
"JNK-mediated turnover and stabilization of the transcription factor
p45/NF-E2 during differentiation of murine erythroleukemia cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:52-57(2010).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21297631; DOI=10.1038/nn.2755;
Westerlund N., Zdrojewska J., Padzik A., Komulainen E., Bjorkblom B.,
Rannikko E., Tararuk T., Garcia-Frigola C., Sandholm J., Nguyen L.,
Kallunki T., Courtney M.J., Coffey E.T.;
"Phosphorylation of SCG10/stathmin-2 determines multipolar stage exit
and neuronal migration rate.";
Nat. Neurosci. 14:305-313(2011).
[16]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22441692; DOI=10.1038/embor.2012.37;
Yoshitane H., Honma S., Imamura K., Nakajima H., Nishide S.Y., Ono D.,
Kiyota H., Shinozaki N., Matsuki H., Wada N., Doi H., Hamada T.,
Honma K., Fukada Y.;
"JNK regulates the photic response of the mammalian circadian clock.";
EMBO Rep. 13:455-461(2012).
-!- FUNCTION: Serine/threonine-protein kinase involved in various
processes such as cell proliferation, differentiation, migration,
transformation and programmed cell death. Extracellular stimuli
such as proinflammatory cytokines or physical stress stimulate the
stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)
signaling pathway. In this cascade, two dual specificity kinases
MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1.
In turn, MAPK8/JNK1 phosphorylates a number of transcription
factors, primarily components of AP-1 such as JUN, JDP2 and ATF2
and thus regulates AP-1 transcriptional activity. Phosphorylates
the replication licensing factor CDT1, inhibiting the interaction
between CDT1 and the histone H4 acetylase HBO1 to replication
origins. Loss of this interaction abrogates the acetylation
required for replication initiation. Promotes stressed cell
apoptosis by phosphorylating key regulatory factors including
p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and
MAPK9 are required for polarized differentiation of T-helper cells
into Th1 cells. Contributes to the survival of erythroid cells by
phosphorylating the antagonist of cell death BAD upon EPO
stimulation. Mediates starvation-induced BCL2 phosphorylation,
BCL2 dissociation from BECN1, and thus activation of autophagy.
Phosphorylates STMN2 and hence regulates microtubule dynamics,
controlling neurite elongation in cortical neurons. In the
developing brain, through its cytoplasmic activity on STMN2,
negatively regulates the rate of exit from multipolar stage and of
radial migration from the ventricular zone (By similarity).
Phosphorylates several other substrates including heat shock
factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3
ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and
plays a role in the regulation of the circadian clock
(PubMed:22441692). Phosphorylates the heat shock transcription
factor HSF1, suppressing HSF1-induced transcriptional activity (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P45983,
ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:11602244,
ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:21297631,
ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:9393873}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9207092};
-!- ENZYME REGULATION: Inhibited by SERPINB3 (By similarity).
Activated by threonine and tyrosine phosphorylation by either of
two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K4 shows a
strong preference for Tyr-185 while MAP2K7 phosphorylates Tyr-183
preferentially. Inhibited by dual specificity phosphatases, such
as DUSP1. {ECO:0000250, ECO:0000269|PubMed:10811224}.
-!- SUBUNIT: Binds to at least four scaffolding proteins,
MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and
SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of
the JNK signaling pathway. Forms a complex with MAPK8IP1 and
ARHGEF28. Interacts with TP53 and WWOX. Interacts with JAMP.
Interacts with NFATC4. Interacts with MECOM; regulates JNK
signaling. Interacts with PIN1; this interaction mediates MAPK8
conformational changes leading to the binding of MAPK8 to its
substrates (By similarity). Interacts with HSF1 (via D domain and
preferentially with hyperphosphorylated form); this interaction
occurs under both normal growth conditions and immediately upon
heat shock (By similarity). Interacts (phosphorylated form) with
NFE2; the interaction phosphorylates NFE2 in undifferentiated
cells. {ECO:0000250, ECO:0000250|UniProtKB:P45983,
ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:11562351,
ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:14499478,
ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:19966288}.
-!- INTERACTION:
P05627:Jun; NbExp=2; IntAct=EBI-298784, EBI-764369;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}.
Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Brain (at protein level).
{ECO:0000269|PubMed:22441692}.
-!- DEVELOPMENTAL STAGE: At 15.5 dpc, mid to low expression throughout
the midbrain, with more prominent levels in the telencephalon,
especially in the intermediate zone, the midbrain roof, the
olfactory epithelium, the inferior colliculus, and the medulla
oblongata. telencephalon revealed concentrated (at protein level).
{ECO:0000269|PubMed:16618812}.
-!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
Levels peak 48 hours after TCR and CD-28 costimulation.
{ECO:0000269|PubMed:10811224}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Phosphorylated by TAOK2 (By similarity). Dually
phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which
activates the enzyme. {ECO:0000250, ECO:0000269|PubMed:11562351}.
-!- DISRUPTION PHENOTYPE: At 14.5 dpc, brain intermediate zone and
cortical plate are significantly thicker in mutant mice compared
to wild type. The number of neuronal cells is increased in the
cortical plate and intermediate zone. Cell cycle exit is decreased
by 13% in the ventricular and subventricular zones. In 17.5 dpc
brains, the ventricular zone was thinner in mutant mice compared
to wild type animals, consistent with the increased number of
neurons in the cortical plate. TUBB3 is consistently more diffuse
and less structured in mutant telencephalon than in wild type.
{ECO:0000269|PubMed:21297631}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
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EMBL; AB005663; BAA85875.1; -; mRNA.
CCDS; CCDS36869.1; -.
RefSeq; NP_057909.1; NM_016700.4.
UniGene; Mm.21495; -.
ProteinModelPortal; Q91Y86; -.
SMR; Q91Y86; -.
BioGrid; 204971; 20.
DIP; DIP-31075N; -.
ELM; Q91Y86; -.
IntAct; Q91Y86; 10.
MINT; MINT-1204569; -.
STRING; 10090.ENSMUSP00000107576; -.
ChEMBL; CHEMBL1795174; -.
iPTMnet; Q91Y86; -.
PhosphoSitePlus; Q91Y86; -.
MaxQB; Q91Y86; -.
PaxDb; Q91Y86; -.
PRIDE; Q91Y86; -.
Ensembl; ENSMUST00000111945; ENSMUSP00000107576; ENSMUSG00000021936.
GeneID; 26419; -.
KEGG; mmu:26419; -.
UCSC; uc007szt.3; mouse.
CTD; 5599; -.
MGI; MGI:1346861; Mapk8.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q91Y86; -.
KO; K04440; -.
PhylomeDB; Q91Y86; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-MMU-139910; Activation of BMF and translocation to mitochondria.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-205043; NRIF signals cell death from the nucleus.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-376172; DSCAM interactions.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:Q91Y86; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000021936; -.
CleanEx; MM_MAPK8; -.
ExpressionAtlas; Q91Y86; baseline and differential.
Genevisible; Q91Y86; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0002102; C:podosome; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0035033; F:histone deacetylase regulator activity; ISO:MGI.
GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0071732; P:cellular response to nitric oxide; IMP:MGI.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:CACAO.
GO; GO:0048263; P:determination of dorsal identity; ISO:MGI.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0007258; P:JUN phosphorylation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0001764; P:neuron migration; IMP:CACAO.
GO; GO:0097150; P:neuronal stem cell population maintenance; ISO:MGI.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0031281; P:positive regulation of cyclase activity; ISO:MGI.
GO; GO:0090045; P:positive regulation of deacetylase activity; ISO:MGI.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0071803; P:positive regulation of podosome assembly; IMP:MGI.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
GO; GO:0097300; P:programmed necrotic cell death; IMP:MGI.
GO; GO:0061833; P:protein localization to tricellular tight junction; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:1902595; P:regulation of DNA replication origin binding; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0009411; P:response to UV; ISO:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008351; MAPK_JNK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01772; JNKMAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Biological rhythms; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Serine/threonine-protein kinase; Transferase.
CHAIN 1 384 Mitogen-activated protein kinase 8.
/FTId=PRO_0000186263.
DOMAIN 26 321 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 32 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 183 185 TXY.
ACT_SITE 151 151 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 55 55 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 116 116 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P49185}.
MOD_RES 183 183 Phosphothreonine; by MAP2K7.
{ECO:0000269|PubMed:11562351}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K4.
{ECO:0000269|PubMed:11562351}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:15345747}.
SEQUENCE 384 AA; 44229 MW; A7320EF933E9CF85 CRC64;
MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER NVAIKKLSRP
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE FQDVYIVMEL MDANLCQVIQ
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF
MMTPYVVTRY YRAPEVILGM GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ
LGTPCPEFMK KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE EWKELIYKEV
MDLEERTKNG VIRGQPSPLA QVQQ


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E1206m ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
E1206r ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
EIAAB24869 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Rat,Rattus norvegicus,Stress-activated protein kinase 4
EIAAB24862 c-Jun N-terminal kinase 3,Jnk3,MAP kinase 10,MAPK 10,Mapk10,Mitogen-activated protein kinase 10,p54-beta,Prkm10,Rat,Rattus norvegicus,SAPK-beta,Stress-activated protein kinase JNK3
EIAAB24858 c-Jun N-terminal kinase 2,Jnk2,MAP kinase 9,MAPK 9,Mapk9,Mitogen-activated protein kinase 9,p54-alpha,Prkm9,Rat,Rattus norvegicus,SAPK-alpha,Stress-activated protein kinase JNK2
E1206r ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206m ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206b ELISA kit Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2 96T
EIAAB24859 Chicken,c-Jun N-terminal kinase 2,Gallus gallus,JNK2,MAP kinase 9,MAPK 9,MAPK9,Mitogen-activated protein kinase 9,Stress-activated protein kinase JNK2
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg


 

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