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Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)

 MP2K1_RAT               Reviewed;         393 AA.
Q01986; Q5EBD5;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 164.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 1;
Short=MAP kinase kinase 1;
Short=MAPKK 1;
EC=2.7.12.2;
AltName: Full=ERK activator kinase 1;
AltName: Full=MAPK/ERK kinase 1;
Short=MEK 1;
Name=Map2k1; Synonyms=Mek1, Prkmk1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=8380494; DOI=10.1073/pnas.90.1.173;
Wu J., Harrison J.K., Vincent L.A., Haystead C., Haystead T.A.J.,
Michel H., Hunt D.F., Lynch K.R., Sturgill T.W.;
"Molecular structure of a protein-tyrosine/threonine kinase activating
p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase.";
Proc. Natl. Acad. Sci. U.S.A. 90:173-177(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8462694; DOI=10.1016/0014-5793(93)80596-M;
Otsu M., Terada Y., Okayama H.;
"Isolation of two members of the rat MAP kinase kinase gene family.";
FEBS Lett. 320:246-250(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley;
PubMed=8406028; DOI=10.1016/0378-1119(93)90312-Q;
Doering F., Drewes G., Berling B., Mandelkow E.M.;
"Cloning and sequencing of a cDNA encoding rat brain mitogen-activated
protein (MAP) kinase activator.";
Gene 131:303-304(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
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]
PROTEIN SEQUENCE OF 206-227; 270-291 AND 325-340, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[6]
DOMAIN, INTERACTION WITH RAF1, AND ENZYME REGULATION.
PubMed=7565670; DOI=10.1128/MCB.15.10.5214;
Catling A.D., Schaeffer H.J., Reuter C.W., Reddy G.R., Weber M.J.;
"A proline-rich sequence unique to MEK1 and MEK2 is required for raf
binding and regulates MEK function.";
Mol. Cell. Biol. 15:5214-5225(1995).
[7]
INTERACTION WITH LAMTOR3, AND ENZYME REGULATION.
PubMed=9733512; DOI=10.1126/science.281.5383.1668;
Schaeffer H.J., Catling A.D., Eblen S.T., Collier L.S., Krauss A.,
Weber M.J.;
"MP1: a MEK binding partner that enhances enzymatic activation of the
MAP kinase cascade.";
Science 281:1668-1671(1998).
[8]
PHOSPHORYLATION, AND FUNCTION.
PubMed=10769026; DOI=10.1083/jcb.149.2.331;
Colanzi A., Deerinck T.J., Ellisman M.H., Malhotra V.;
"A specific activation of the mitogen-activated protein kinase kinase
1 (MEK1) is required for Golgi fragmentation during mitosis.";
J. Cell Biol. 149:331-339(2000).
[9]
INTERACTION WITH ARRB2.
PubMed=11226259; DOI=10.1073/pnas.041604898;
Luttrell L.M., Roudabush F.L., Choy E.W., Miller W.E., Field M.E.,
Pierce K.L., Lefkowitz R.J.;
"Activation and targeting of extracellular signal-regulated kinases by
beta-arrestin scaffolds.";
Proc. Natl. Acad. Sci. U.S.A. 98:2449-2454(2001).
[10]
PHOSPHORYLATION AT SER-298, AND ENZYME REGULATION.
PubMed=12876277; DOI=10.1083/jcb.200212141;
Slack-Davis J.K., Eblen S.T., Zecevic M., Boerner S.A.,
Tarcsafalvi A., Diaz H.B., Marshall M.S., Weber M.J., Parsons J.T.,
Catling A.D.;
"PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK
activation.";
J. Cell Biol. 162:281-291(2003).
[11]
PHOSPHORYLATION AT THR-292 AND SER-298, INTERACTION WITH MAPK1/ERK2,
AND ENZYME REGULATION.
PubMed=14993270; DOI=10.1128/MCB.24.6.2308-2317.2004;
Eblen S.T., Slack-Davis J.K., Tarcsafalvi A., Parsons J.T.,
Weber M.J., Catling A.D.;
"Mitogen-activated protein kinase feedback phosphorylation regulates
MEK1 complex formation and activation during cellular adhesion.";
Mol. Cell. Biol. 24:2308-2317(2004).
[12]
FUNCTION OF THE MAPK/ERK PATHWAY.
PubMed=19177150; DOI=10.1038/emboj.2008.308;
Nada S., Hondo A., Kasai A., Koike M., Saito K., Uchiyama Y.,
Okada M.;
"The novel lipid raft adaptor p18 controls endosome dynamics by
anchoring the MEK-ERK pathway to late endosomes.";
EMBO J. 28:477-489(2009).
[13]
IDENTIFICATION IN A COMPLEX WITH BRAF; HRAS; MAPK3 AND RGS14.
PubMed=19319189; DOI=10.1371/journal.pone.0004884;
Willard F.S., Willard M.D., Kimple A.J., Soundararajan M.,
Oestreich E.A., Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J.,
Zylka M.J., Snider W.D., Siderovski D.P.;
"Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
effector.";
PLoS ONE 4:E4884-E4884(2009).
[14]
REVIEW ON FUNCTION.
PubMed=9779990; DOI=10.1038/sj.onc.1202251;
Dhanasekaran N., Premkumar Reddy E.;
"Signaling by dual specificity kinases.";
Oncogene 17:1447-1455(1998).
[15]
REVIEW ON ENZYME REGULATION.
PubMed=15520807; DOI=10.1038/nrm1498;
Wellbrock C., Karasarides M., Marais R.;
"The RAF proteins take centre stage.";
Nat. Rev. Mol. Cell Biol. 5:875-885(2004).
[16]
REVIEW ON FUNCTION.
PubMed=19565474; DOI=10.1002/biof.52;
Yao Z., Seger R.;
"The ERK signaling cascade--views from different subcellular
compartments.";
BioFactors 35:407-416(2009).
[17]
REVIEW ON FUNCTION.
PubMed=21779493; DOI=10.1177/1947601911407328;
Wortzel I., Seger R.;
"The ERK cascade: distinct functions within various subcellular
organelles.";
Genes Cancer 2:195-209(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Dual specificity protein kinase which acts as an
essential component of the MAP kinase signal transduction pathway.
Binding of extracellular ligands such as growth factors, cytokines
and hormones to their cell-surface receptors activates RAS and
this initiates RAF1 activation. RAF1 then further activates the
dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both
MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK
cascade, and catalyze the concomitant phosphorylation of a
threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located
in the extracellular signal-regulated kinases MAPK3/ERK1 and
MAPK1/ERK2, leading to their activation and further transduction
of the signal within the MAPK/ERK cascade. Depending on the
cellular context, this pathway mediates diverse biological
functions such as cell growth, adhesion, survival and
differentiation, predominantly through the regulation of
transcription, metabolism and cytoskeletal rearrangements. One
target of the MAPK/ERK cascade is peroxisome proliferator-
activated receptor gamma (PPARG), a nuclear receptor that promotes
differentiation and apoptosis. MAP2K1/MEK1 has been shown to
export PPARG from the nucleus. The MAPK/ERK cascade is also
involved in the regulation of endosomal dynamics, including
lysosome processing and endosome cycling through the perinuclear
recycling compartment (PNRC), as well as in the fragmentation of
the Golgi apparatus during mitosis. {ECO:0000269|PubMed:10769026,
ECO:0000269|PubMed:19177150}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Ras proteins such as HRAS mediate the
activation of RAF proteins such as RAF1 or BRAF which in turn
activate extracellular signal-regulated kinases (ERK) through MAPK
(mitogen-activated protein kinases) and ERK kinases MAP2K1/MEK1
and MAP2K2/MEK2. Activation occurs through phosphorylation of Ser-
218 and Ser-222. MAP2K1/MEK1 is also the target of negative feed-
back regulation by its substrate kinases, such as MAPK1/ERK2.
These phosphorylate MAP2K1/MEK1 on Thr-292, thereby facilitating
dephosphorylation of the activating residues Ser-218 and Ser-222.
Inhibited by serine/threonine phosphatase 2A.
{ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14993270,
ECO:0000269|PubMed:7565670, ECO:0000269|PubMed:9733512}.
-!- SUBUNIT: Forms a heterodimer with MAP2K2/MEK2. Forms heterodimers
with KSR2 which further dimerize to form tetramers. Interacts with
MORG1 and VRK2. Interacts with SGK1, BIRC6/bruce and KSR1 (By
similarity). Found in a complex with at least BRAF, HRAS,
MAPK3/ERK1 and RGS14 (PubMed:19319189). Interacts with ARRB2,
LAMTOR3, MAPK1/ERK2, and RAF1 (via the proline-rich domain)
(PubMed:7565670, PubMed:9733512, PubMed:11226259,
PubMed:14993270). {ECO:0000250|UniProtKB:P29678,
ECO:0000250|UniProtKB:P31938, ECO:0000250|UniProtKB:Q02750,
ECO:0000269|PubMed:11226259, ECO:0000269|PubMed:19319189,
ECO:0000269|PubMed:7565670, ECO:0000269|PubMed:9733512}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:Q02750}.
Cytoplasm, cytoskeleton, microtubule organizing center, spindle
pole body {ECO:0000250|UniProtKB:Q02750}. Cytoplasm
{ECO:0000250|UniProtKB:Q02750}. Nucleus
{ECO:0000250|UniProtKB:Q02750}. Membrane
{ECO:0000250|UniProtKB:Q02750}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q02750}. Note=Localizes at centrosomes
during prometaphase, midzone during anaphase and midbody during
telophase/cytokinesis. Membrane localization is probably regulated
by its interaction with KSR1. {ECO:0000250|UniProtKB:Q02750}.
-!- DOMAIN: The proline-rich region localized between residues 270 and
307 is important for binding to RAF1 and activation of
MAP2K1/MEK1. {ECO:0000269|PubMed:7565670}.
-!- PTM: Phosphorylation at Ser-218 and Ser-222 by MAP kinase kinase
kinases (RAF or MEKK1) positively regulates kinase activity. Also
phosphorylated at Thr-292 by MAPK1/ERK2 and at Ser-298 by PAK.
MAPK1/ERK2 phosphorylation of Thr-292 occurs in response to
cellular adhesion and leads to inhibition of Ser-298
phosphorylation by PAK. {ECO:0000269|PubMed:10769026,
ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14993270}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; Z16415; CAA78905.1; -; mRNA.
EMBL; D13341; BAA02603.1; -; mRNA.
EMBL; D14591; BAA03441.1; -; mRNA.
EMBL; X62313; CAA44192.1; -; mRNA.
EMBL; BC089772; AAH89772.1; -; mRNA.
PIR; JN0840; JN0840.
RefSeq; NP_113831.1; NM_031643.4.
UniGene; Rn.5850; -.
ProteinModelPortal; Q01986; -.
SMR; Q01986; -.
BioGrid; 251005; 6.
STRING; 10116.ENSRNOP00000013933; -.
iPTMnet; Q01986; -.
PhosphoSitePlus; Q01986; -.
PaxDb; Q01986; -.
PRIDE; Q01986; -.
GeneID; 170851; -.
KEGG; rno:170851; -.
UCSC; RGD:70495; rat.
CTD; 5604; -.
RGD; 70495; Map2k1.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; Q01986; -.
KO; K04368; -.
OrthoDB; EOG091G0DEC; -.
PhylomeDB; Q01986; -.
TreeFam; TF105137; -.
BRENDA; 2.7.12.2; 5301.
PRO; PR:Q01986; -.
Proteomes; UP000002494; Unplaced.
Genevisible; Q01986; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005938; C:cell cortex; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005925; C:focal adhesion; TAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005770; C:late endosome; TAS:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:RGD.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IDA:RGD.
GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0017016; F:Ras GTPase binding; IPI:RGD.
GO; GO:0004728; F:signal transducer, downstream of receptor, with protein tyrosine phosphatase activity; ISO:RGD.
GO; GO:0000187; P:activation of MAPK activity; IDA:RGD.
GO; GO:0060020; P:Bergmann glial cell differentiation; ISO:RGD.
GO; GO:0007050; P:cell cycle arrest; ISO:RGD.
GO; GO:0048870; P:cell motility; ISO:RGD.
GO; GO:0008283; P:cell proliferation; IDA:RGD.
GO; GO:0090398; P:cellular senescence; ISO:RGD.
GO; GO:0021697; P:cerebellar cortex formation; ISO:RGD.
GO; GO:0060502; P:epithelial cell proliferation involved in lung morphogenesis; ISO:RGD.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0060324; P:face development; ISO:RGD.
GO; GO:0042593; P:glucose homeostasis; IDA:RGD.
GO; GO:0048313; P:Golgi inheritance; IMP:RGD.
GO; GO:0007507; P:heart development; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
GO; GO:0060711; P:labyrinthine layer development; ISO:RGD.
GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
GO; GO:0000165; P:MAPK cascade; IMP:RGD.
GO; GO:0032402; P:melanosome transport; IDA:RGD.
GO; GO:0000278; P:mitotic cell cycle; IDA:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; IMP:RGD.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IMP:CAFA.
GO; GO:0030182; P:neuron differentiation; IMP:RGD.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
GO; GO:0060674; P:placenta blood vessel development; ISO:RGD.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:CAFA.
GO; GO:0010508; P:positive regulation of autophagy; IDA:RGD.
GO; GO:0050772; P:positive regulation of axonogenesis; ISO:RGD.
GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:RGD.
GO; GO:0045933; P:positive regulation of muscle contraction; IMP:CAFA.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:RGD.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:MGI.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0051291; P:protein heterooligomerization; IPI:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0048679; P:regulation of axon regeneration; ISO:RGD.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:RGD.
GO; GO:0090170; P:regulation of Golgi inheritance; TAS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
GO; GO:0003056; P:regulation of vascular smooth muscle contraction; IMP:RGD.
GO; GO:0048678; P:response to axon injury; IMP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
GO; GO:0048538; P:thymus development; ISO:RGD.
GO; GO:0030878; P:thyroid gland development; ISO:RGD.
GO; GO:0060440; P:trachea formation; ISO:RGD.
GO; GO:0070328; P:triglyceride homeostasis; IDA:RGD.
GO; GO:0047496; P:vesicle transport along microtubule; IDA:RGD.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Kinase; Membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
CHAIN 1 393 Dual specificity mitogen-activated
protein kinase kinase 1.
/FTId=PRO_0000086369.
DOMAIN 68 361 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 74 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 270 307 RAF1-binding.
COMPBIAS 262 307 Pro-rich.
ACT_SITE 190 190 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 97 97 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 8 9 Cleavage; by anthrax lethal factor.
{ECO:0000250}.
MOD_RES 218 218 Phosphoserine; by RAF.
{ECO:0000250|UniProtKB:Q02750}.
MOD_RES 222 222 Phosphoserine; by RAF.
{ECO:0000250|UniProtKB:Q02750}.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02750}.
MOD_RES 292 292 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:14993270}.
MOD_RES 298 298 Phosphoserine; by PAK.
{ECO:0000269|PubMed:12876277,
ECO:0000269|PubMed:14993270}.
SEQUENCE 393 AA; 43465 MW; A1C8D18FFC852D51 CRC64;
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV
GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE
CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL
REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY
SVQSDIWSMG LSLVEMAVGR YPIPPPDAKE LELLFGCQVE GDAAETPPRP RTPGRPLSSY
GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF
IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA ASI


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10-782-55047 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.05 mg
10-782-55047 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.02 mg
10-782-55048 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.05 mg
EIAAB25230 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,MAP kinase kinase 1,Map2k1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,Mek1,Mouse,Mus musculus,Prkmk1
EIAAB25228 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,MAP kinase kinase 1,Map2k1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,Mek1,Prkmk1,Rat,Rattus norvegicus
EIAAB25234 Dual specificity mitogen-activated protein kinase kinase 2,ERK activator kinase 2,MAP kinase kinase 2,Map2k2,MAPK_ERK kinase 2,MAPKK 2,MEK 2,Mek2,Mkk2,Prkmk2,Rat,Rattus norvegicus
EIAAB25236 Dual specificity mitogen-activated protein kinase kinase 2,ERK activator kinase 2,MAP kinase kinase 2,Map2k2,MAPK_ERK kinase 2,MAPKK 2,MEK 2,Mek2,Mkk2,Mouse,Mus musculus,Prkmk2
EIAAB25229 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,MAP kinase kinase 1,MAP2K1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,MEK1,Oryctolagus cuniculus,PRKMK1,Rabbit
EIAAB25231 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,Homo sapiens,Human,MAP kinase kinase 1,MAP2K1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,MEK1,MKK1,PRKMK1
EIAAB25235 Dual specificity mitogen-activated protein kinase kinase 2,ERK activator kinase 2,Homo sapiens,Human,MAP kinase kinase 2,MAP2K2,MAPK_ERK kinase 2,MAPKK 2,MEK 2,MEK2,MKK2,PRKMK2
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB25232 Chicken,Dual specificity mitogen-activated protein kinase kinase 2,ERK activator kinase 2,Gallus gallus,MAP kinase kinase 2,MAP2K2,MAPK_ERK kinase 2,MAPKK 2,MEK2,MEK2,MKK2,PRKMK2
EIAAB25233 Canis familiaris,Canis lupus familiaris,Dog,Dual specificity mitogen-activated protein kinase kinase 2,ERK activator kinase 2,MAP kinase kinase 2,MAP2K2,MAPK_ERK kinase 2,MAPKK 2,MEK 2,MEK2
E1721b ELISA kit Bos taurus,Bovine,Dual specificity mitogen-activated protein kinase kinase 6,MAP kinase kinase 6,MAP2K6,MAPK_ERK kinase 6,MAPKK 6,MEK 6 96T
E1721b ELISA Bos taurus,Bovine,Dual specificity mitogen-activated protein kinase kinase 6,MAP kinase kinase 6,MAP2K6,MAPK_ERK kinase 6,MAPKK 6,MEK 6 96T
U1721b CLIA Bos taurus,Bovine,Dual specificity mitogen-activated protein kinase kinase 6,MAP kinase kinase 6,MAP2K6,MAPK_ERK kinase 6,MAPKK 6,MEK 6 96T


 

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