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

Rho guanine nucleotide exchange factor 28 (190 kDa guanine nucleotide exchange factor) (p190-RhoGEF) (p190RhoGEF) (Rho guanine nucleotide exchange factor) (Rho-interacting protein 2)

 ARG28_MOUSE             Reviewed;        1693 AA.
P97433; A0PJC1; Q69Z41; Q6DI55;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
23-MAY-2018, entry version 143.
RecName: Full=Rho guanine nucleotide exchange factor 28;
AltName: Full=190 kDa guanine nucleotide exchange factor;
Short=p190-RhoGEF;
Short=p190RhoGEF;
AltName: Full=Rho guanine nucleotide exchange factor;
AltName: Full=Rho-interacting protein 2;
Name=Arhgef28; Synonyms=Kiaa1998, Rgnef, Rhoip2, Rip2;
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 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=9199174; DOI=10.1083/jcb.137.7.1603;
Gebbink M.F.B.G., Kranenburg O., Poland M., van Horck F.P.G.,
Houssa B., Moolenaar W.H.;
"Identification of a novel, putative Rho-specific GDP/GTP exchange
factor and a RhoA-binding protein: control of neuronal morphology.";
J. Cell Biol. 137:1603-1613(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-649 (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Bone, and 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).
[4]
INTERACTION WITH MAPK8IP1, AND MUTAGENESIS OF PHE-1563; ASN-1565 AND
PHE-1568.
PubMed=10574993; DOI=10.1074/jbc.274.49.35113;
Meyer D., Liu A., Margolis B.;
"Interaction of c-Jun amino-terminal kinase interacting protein-1 with
p190 rhoGEF and its localization in differentiated neurons.";
J. Biol. Chem. 274:35113-35118(1999).
[5]
FUNCTION, INTERACTION WITH RHOA AND MICROTUBULES, MUTAGENESIS OF
TYR-1003, AND SUBCELLULAR LOCATION.
PubMed=11058585; DOI=10.1074/jbc.M003839200;
van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H.,
Kranenburg O.;
"Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide
exchange factor that interacts with microtubules.";
J. Biol. Chem. 276:4948-4956(2001).
[6]
FUNCTION IN NEFL EXPRESSION, AND NEFL RNA-BINDING.
PubMed=11435431; DOI=10.1074/jbc.M104104200;
Canete-Soler R., Wu J., Zhai J., Shamim M., Schlaepfer W.W.;
"p190RhoGEF Binds to a destabilizing element in the 3' untranslated
region of light neurofilament subunit mRNA and alters the stability of
the transcript.";
J. Biol. Chem. 276:32046-32050(2001).
[7]
INTERACTION WITH YWHAE AND YWHAH, AND MUTAGENESIS OF ASN-1375 AND
LEU-1376.
PubMed=11533041; DOI=10.1074/jbc.M107709200;
Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
"Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
J. Biol. Chem. 276:41318-41324(2001).
[8]
FUNCTION, OLIGOMERIZATION, AND IDENTIFICATION IN A COMPLEX WITH MAPK8
AND MAPK8IP1.
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).
[9]
FUNCTION, INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION, AND TISSUE
SPECIFICITY.
PubMed=12702722; DOI=10.1074/jbc.M302381200;
Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W.,
Schlaepfer D.D.;
"Direct interaction of focal adhesion kinase with p190RhoGEF.";
J. Biol. Chem. 278:24865-24873(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INDUCTION.
PubMed=12496377; DOI=10.4049/jimmunol.170.1.19;
Lee J.R., Ha Y.J., Kim H.J.;
"Induced expression of a RhoA-specific guanine nucleotide exchange
factor, p190RhoGEF, following CD40 stimulation and WEHI 231 B cell
activation.";
J. Immunol. 170:19-23(2003).
[11]
FUNCTION IN AXONAL BRANCHING AND SYNAPSE FORMATION.
PubMed=15378065; DOI=10.1038/nn1317;
Rico B., Beggs H.E., Schahin-Reed D., Kimes N., Schmidt A.,
Reichardt L.F.;
"Control of axonal branching and synapse formation by focal adhesion
kinase.";
Nat. Neurosci. 7:1059-1069(2004).
[12]
FUNCTION, AND INTERACTION WITH NEFL.
PubMed=16236762; DOI=10.1093/hmg/ddi392;
Lin H., Zhai J., Schlaepfer W.W.;
"RNA-binding protein is involved in aggregation of light neurofilament
protein and is implicated in the pathogenesis of motor neuron
degeneration.";
Hum. Mol. Genet. 14:3643-3659(2005).
[13]
FUNCTION, AND INTERACTION WITH CTNND2.
PubMed=17993462; DOI=10.1074/jbc.M707158200;
Kim H., Han J.-R., Park J., Oh M., James S.E., Chang S., Lu Q.,
Lee K.Y., Ki H., Song W.-J., Kim K.;
"Delta-catenin-induced dendritic morphogenesis. An essential role of
p190RhoGEF interaction through Akt1-mediated phosphorylation.";
J. Biol. Chem. 283:977-987(2008).
[14]
FUNCTION, AND INDUCTION BY PTK2B/PYK2.
PubMed=18195107; DOI=10.1083/jcb.200708194;
Lim Y., Lim S.-T., Tomar A., Gardel M., Bernard-Trifilo J.A.,
Chen X.L., Uryu S.A., Canete-Soler R., Zhai J., Lin H.,
Schlaepfer W.W., Nalbant P., Bokoch G., Ilic D., Waterman-Storer C.,
Schlaepfer D.D.;
"PyK2 and FAK connections to p190Rho guanine nucleotide exchange
factor regulate RhoA activity, focal adhesion formation, and cell
motility.";
J. Cell Biol. 180:187-203(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1604, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, and Pancreas;
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).
-!- FUNCTION: Functions as a RHOA-specific guanine nucleotide exchange
factor regulating signaling pathways downstream of integrins and
growth factor receptors. Functions in axonal branching, synapse
formation and dendritic morphogenesis. Functions also in focal
adhesion formation, cell motility and B-lymphocytes activation.
May regulate NEFL expression and aggregation and play a role in
apoptosis. {ECO:0000269|PubMed:11058585,
ECO:0000269|PubMed:11435431, ECO:0000269|PubMed:12496377,
ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:14499478,
ECO:0000269|PubMed:15378065, ECO:0000269|PubMed:16236762,
ECO:0000269|PubMed:17993462, ECO:0000269|PubMed:18195107,
ECO:0000269|PubMed:9199174}.
-!- SUBUNIT: Homooligomer; forms some cytoplasmic aggregates. Forms a
complex with MAPK8 and MAPK8IP1. Interacts with RHOA. Interacts
with microtubules. Interacts with YWHAE and YWHAH. Interacts with
PTK2/FAK1. Interacts with NEFL. Interacts with CTNND2; prevents
interaction with RHOA. {ECO:0000269|PubMed:10574993,
ECO:0000269|PubMed:11058585, ECO:0000269|PubMed:11533041,
ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:14499478,
ECO:0000269|PubMed:16236762, ECO:0000269|PubMed:17993462}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Colocalizes
with the microtubule radial and cortical systems.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P97433-1; Sequence=Displayed;
Name=2;
IsoId=P97433-2; Sequence=VSP_032145, VSP_032146;
-!- TISSUE SPECIFICITY: Highly enriched in the brain (at protein
level). Also detected in lung and kidney.
{ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:9199174}.
-!- INDUCTION: Up-regulated in B-lymphocytes upon CD40 stimulation.
Up-regulated by PTK2B/PYK2 (at protein level).
{ECO:0000269|PubMed:12496377, ECO:0000269|PubMed:18195107}.
-!- PTM: Phosphorylated on tyrosine upon stimulation of cells by
laminin. {ECO:0000269|PubMed:12702722}.
-!- SEQUENCE CAUTION:
Sequence=AAH22978.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH75734.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAD32603.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U73199; AAB18197.1; -; mRNA.
EMBL; AK173325; BAD32603.1; ALT_INIT; mRNA.
EMBL; BC022978; AAH22978.1; ALT_SEQ; mRNA.
EMBL; BC075734; AAH75734.1; ALT_SEQ; mRNA.
PIR; T30867; T30867.
RefSeq; NP_036156.2; NM_012026.2.
UniGene; Mm.252718; -.
ProteinModelPortal; P97433; -.
SMR; P97433; -.
IntAct; P97433; 2.
MINT; P97433; -.
STRING; 10090.ENSMUSP00000105053; -.
iPTMnet; P97433; -.
PhosphoSitePlus; P97433; -.
MaxQB; P97433; -.
PaxDb; P97433; -.
PRIDE; P97433; -.
GeneID; 110596; -.
KEGG; mmu:110596; -.
UCSC; uc007rol.1; mouse. [P97433-2]
CTD; 64283; -.
MGI; MGI:1346016; Arhgef28.
eggNOG; KOG3519; Eukaryota.
eggNOG; KOG3520; Eukaryota.
eggNOG; ENOG410XT68; LUCA.
HOGENOM; HOG000154109; -.
HOVERGEN; HBG079129; -.
InParanoid; P97433; -.
KO; K21072; -.
PhylomeDB; P97433; -.
ChiTaRS; Arhgef28; mouse.
PRO; PR:P97433; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_RGNEF; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
CDD; cd00029; C1; 1.
CDD; cd14680; PH_p190RhoGEF; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR037819; ARHGEF28_PH.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00130; C1_1; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Coiled coil; Complete proteome;
Cytoplasm; Differentiation; Guanine-nucleotide releasing factor;
Membrane; Metal-binding; Phosphoprotein; Reference proteome;
RNA-binding; Zinc; Zinc-finger.
CHAIN 1 1693 Rho guanine nucleotide exchange factor
28.
/FTId=PRO_0000080967.
DOMAIN 846 1041 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 1095 1184 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 651 698 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 1292 1301 Interaction with PTK2/FAK1; required for
regulation of axonal branching and
synapse formation.
REGION 1369 1380 Mediates cytoplasmic retention and
interaction with YWHAH.
{ECO:0000269|PubMed:11533041}.
REGION 1421 1693 Interaction with microtubules.
REGION 1493 1524 RNA-binding. {ECO:0000250}.
REGION 1563 1576 Mediates cytoplasmic retention and
interaction with MAPK8IP1.
{ECO:0000269|PubMed:10574993}.
COILED 1421 1522 {ECO:0000255}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000250|UniProtKB:P0C6P5}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:P0C6P5}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000250|UniProtKB:P0C6P5}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N1W1}.
MOD_RES 1535 1535 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N1W1}.
MOD_RES 1604 1604 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1322 1324 SLV -> CGI (in isoform 2).
{ECO:0000303|PubMed:15368895}.
/FTId=VSP_032145.
VAR_SEQ 1325 1693 Missing (in isoform 2).
{ECO:0000303|PubMed:15368895}.
/FTId=VSP_032146.
MUTAGEN 1003 1003 Y->A: Loss of function.
{ECO:0000269|PubMed:11058585}.
MUTAGEN 1375 1375 N->A: Alters interaction with YWHAH.
{ECO:0000269|PubMed:11533041}.
MUTAGEN 1376 1376 L->A: Alters interaction with YWHAH.
{ECO:0000269|PubMed:11533041}.
MUTAGEN 1563 1563 F->A: Alters interaction with MAPK8IP1.
{ECO:0000269|PubMed:10574993}.
MUTAGEN 1565 1565 N->A: Alters interaction with MAPK8IP1.
{ECO:0000269|PubMed:10574993}.
MUTAGEN 1568 1568 F->A: Alters interaction with MAPK8IP1.
{ECO:0000269|PubMed:10574993}.
CONFLICT 340 340 A -> P (in Ref. 3; AAH75734).
{ECO:0000305}.
CONFLICT 481 481 A -> T (in Ref. 3; AAH75734).
{ECO:0000305}.
SEQUENCE 1693 AA; 190326 MW; 4E96087C449FF14C CRC64;
MELSCSEVPL YGQKTVYAKF GKNVYLPEDA EFYFVYGGSH QRHVVIADRV QDNVLQSSIP
GHWLQETVTV SVCLCSEGYS PVTMGSGSVT YVDNMACRLA RLLVTQADRL TACSHQTLLT
PFALTVEALP ALDEELVLAL TQLELPLGWT VLGNSSLEVS LHRESLLHLA VRWALPKLFH
FLLCLPGGVK ALKLPNEEAT TPLDLALQGG HSTLVEDITN FQGSHSPGFS RLRLNEEATL
QFVHSSETLT LTVNHTAEHL LEADIKLFRK YFWDRAFLVK ALEQEAKTEK ATMPSGAAET
EEEVRNLESG RSPSEEEEDA KSIKSQVDGP SEHEDQDRLA LDRSFDGLKK SKHVPASLAA
GQLSDVLNGG DEVYANCMVI DQVGDLDINY INLEGLSTHT SPESGRSMLG PQACMHTLPP
DTSPCGRPLI ENSEGTLDAA ASQSFVTPSS SRTSNLNLSF GLHGFEKEQS HLKKRSSSLD
ALVADSEGEG GSEPPICYAV GSQSSPRTGL PSGDELDSFE TNTEPDCNIS RTESLSLSST
LHSKESLLSG IRSRSYSCSS PKISSGKSRL VRDFTVCSTS EEQRSYSFQE PPGEKRIQEE
EWDEYVIPAK SESEKYKVSR TFSFLMNRMT SPRNKSKMKN KDTKEKEKMN RHQFVPGTFS
GVLQCSGCDK TLLGKESLQC ANCKANTHKG CKDAVPPCTK KFQEKYNKNK PQSILGSSSV
RDVPAPGLSL HPSSSMPIGL PAGRKEFAAQ VHPLSRSVPG TTLESFRRAV TSLESEGDSW
RSRSHSDELF QSMGSSPSTE SFMMEDVVDS SLWIDLSSDA QEFEAESWSL VVDPSFCSRQ
EKDVIKRQDV IFELMQTEVH HIQTLLIMSE VFRKGMKEEL QLDHSTVDKI FPCLDELLET
HRHFFFSMKE RRQESCAGSD RNFVINQIGD ILVQQFSEEN ASKMKRIYGE FCSHHKEAMS
LFKELQQNKK FQNFIKIRNS NLLARRRGIP ECILLVTQRI TKYPVLVERI LQYTKERTEE
HRDLCKALGL IKDMIAAVDL KVSEYEKNQK WLEILNKIEN KTYTKLKNGH VFRKQALLSQ
ERALLHDGLV YWKTATGRFK DILALLLTDV LLFLQEKDQK YIFAAVDQKP SVISLQKLIA
REVANEERGM FLISASSAGP EMYEIHTNSK EERNNWMRRI QQAVESCPEE EGGRTSESDE
ERRKAEARVA KIQQCQEILS NQDQQICTYL EEKLHIYAEL GELSGFEDVH LEPHLLIKPD
PGEPPQAASL LAAALREAES LQVAVKASKM GDVSQSSEES PGGTVLMDTP STQDVPASPT
ASLVTEGTEG RGCWDVDPGL QGVVTDLAVS DAGEKVEYRS FSGSSQSEII QAIQNLTRLL
YSLQAALTIQ DSHIEIHKLV LQQRESLAPS HSFRGGPLQD QEKSRYLEKQ REELANIHKL
QHQFQQEQRR WHRTCDQQQR EQEAQESWLQ ARERECQSQE ELLLRHRSEL DHQLQEYQQS
LERLREGQRM VERERQKMRV QQGLLGHCKH SRQRSLPAVF SPGSKEVTEL NRAESLCHEN
SFFINEAFGH MSLNTSNKPN PSGVPWDAHP LEGSHFDLAR TSESPTELKI DISQPPDVNS
ELWTTGPGHQ RPALQENSKE SYKNVADLDS FQSESSSPQD SNQRWPPATD THNRSKTKSS
DGGWTRWRCW RRG


Related products :

Catalog number Product name Quantity
EIAAB34493 190 kDa guanine nucleotide exchange factor,Kiaa1998,Mouse,Mus musculus,p190RhoGEF,p190-RhoGEF,Rgnef,Rho-guanine nucleotide exchange factor,Rho-interacting protein 2,Rhoip2,Rip2
EIAAB34494 190 kDa guanine nucleotide exchange factor,Homo sapiens,Human,KIAA1998,p190RhoGEF,p190-RhoGEF,RGNEF,Rho-guanine nucleotide exchange factor
EIAAB34495 190 kDa guanine nucleotide exchange factor,p190RhoGEF,p190-RhoGEF,Rat,Rattus norvegicus,Rgnef,Rho-guanine nucleotide exchange factor
EIAAB35857 Kiaa0313,Mouse,Mus musculus,Neural RAP guanine nucleotide exchange protein,nRap GEP,PDZ domain-containing guanine nucleotide exchange factor 1,Pdzgef1,PDZ-GEF1,Rap guanine nucleotide exchange factor 2
EIAAB35856 Homo sapiens,Human,KIAA0313,Neural RAP guanine nucleotide exchange protein,nRap GEP,NRAPGEP,PDZ domain-containing guanine nucleotide exchange factor 1,PDZGEF1,PDZ-GEF1,RA-GEF,Rap guanine nucleotide ex
EIAAB39882 Deafness locus-associated putative guanine nucleotide exchange factor,DelGEF,DELGEF,GNEFR,Guanine nucleotide exchange factor-related protein,Homo sapiens,Human,Secretion-regulating guanine nucleotide
EIAAB39884 Deafness locus-associated putative guanine nucleotide exchange factor,DelGEF,Delgef,Gnefr,Guanine nucleotide exchange factor-related protein,Mouse,Mus musculus,Secretion-regulating guanine nucleotide
EIAAB35861 cAMP-dependent Rap1 guanine-nucleotide exchange factor,cAMP-GEFII,cAMP-regulated guanine nucleotide exchange factor II,Cgef2,EPAC 2,Epac2,Exchange factor directly activated by cAMP 2,Exchange protein
EIAAB35866 GFR,Guanine nucleotide exchange factor for Rap1,Homo sapiens,Human,KIAA0277,M-Ras-regulated Rap GEF,MRGEF,MR-GEF,Rap guanine nucleotide exchange factor 5,RAPGEF5,Related to Epac,Repac
EIAAB35865 Gfr,Guanine nucleotide exchange factor for Rap1,Kiaa0277,Mouse,M-Ras-regulated Rap GEF,Mrgef,MR-GEF,Mus musculus,Rap guanine nucleotide exchange factor 5,Rapgef5
EIAAB35867 Homo sapiens,Human,PDZ domain-containing guanine nucleotide exchange factor 2,PDZGEF2,PDZ-GEF2,RA-GEF-2,Rap guanine nucleotide exchange factor 6,RAPGEF6
EIAAB35869 Homo sapiens,Human,Link GEFII,Link guanine nucleotide exchange factor II,Rap guanine nucleotide exchange factor-like 1,RAPGEFL1
EIAAB35855 CRK SH3-binding GNRP,GRF2,Guanine nucleotide-releasing factor 2,Homo sapiens,Human,Protein C3G,Rap guanine nucleotide exchange factor 1,RAPGEF1
20-372-60216 deafness locus associated putative guanine nucleotide exchange factor (DELGEF) - Mouse monoclonal anti-human DELGEF antibody; Guanine nucleotide exchange factor-related protein; Deafness locus-associa 0.1 mg
EIAAB35862 cAMP-GEFII,cAMP-regulated guanine nucleotide exchange factor II,Cgef2,EPAC 2,Epac2,Exchange factor directly activated by cAMP 2,Exchange protein directly activated by cAMP 2,Rap guanine nucleotide exc
EIAAB27125 Ephexin-1,Eph-interacting exchange protein,Mouse,Mus musculus,Neuronal guanine nucleotide exchange factor,Ngef
EIAAB27123 Ephexin-1,Eph-interacting exchange protein,Neuronal guanine nucleotide exchange factor,Ngef,Rat,Rattus norvegicus
EIAAB27124 Ephexin-1,Eph-interacting exchange protein,Homo sapiens,Human,Neuronal guanine nucleotide exchange factor,NGEF
EIAAB34512 Kiaa0351,Mouse,Mus musculus,Ral GEF with PH domain and SH3-binding motif 1,Ral guanine nucleotide exchange factor 2,RalA exchange factor RalGPS1,RalGEF 2,Ralgef2,Ralgps1,Ralgps1a,Ras-specific guanine
EIAAB34513 Homo sapiens,Human,KIAA0351,Ral GEF with PH domain and SH3-binding motif 1,Ral guanine nucleotide exchange factor 2,RalA exchange factor RalGPS1,RalGEF 2,RALGEF2,RALGPS1,Ras-specific guanine nucleotid
EIAAB35860 cAMP-GEFI,cAMP-regulated guanine nucleotide exchange factor I,Epac,EPAC 1,Epac1,Exchange factor directly activated by cAMP 1,Exchange protein directly activated by cAMP 1,Rap guanine nucleotide exchan
EIAAB34523 GRF2,Homo sapiens,Human,Ras guanine nucleotide exchange factor 2,RASGRF2,Ras-GRF2,Ras-specific guanine nucleotide-releasing factor 2
EIAAB34524 Grf2,Mouse,Mus musculus,Ras guanine nucleotide exchange factor 2,Rasgrf2,Ras-GRF2,Ras-specific guanine nucleotide-releasing factor 2
EIAAB34522 Grf2,Ras guanine nucleotide exchange factor 2,Rasgrf2,Ras-GRF2,Ras-specific guanine nucleotide-releasing factor 2,Rat,Rattus norvegicus
EIAAB34519 Cdc25,CDC25Mm,GNRP,Grf1,Guanine nucleotide-releasing protein,Mouse,Mus musculus,Rasgrf1,Ras-GRF1,Ras-specific guanine nucleotide-releasing factor 1,Ras-specific nucleotide exchange factor CDC25


 

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