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Macrophage-stimulating protein receptor (MSP receptor) (EC 2.7.10.1) (CDw136) (Protein-tyrosine kinase 8) (p185-Ron) (CD antigen CD136) [Cleaved into: Macrophage-stimulating protein receptor alpha chain; Macrophage-stimulating protein receptor beta chain]

 RON_HUMAN               Reviewed;        1400 AA.
Q04912; B5A944; B5A945; B5A946; B5A947;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 2.
22-NOV-2017, entry version 187.
RecName: Full=Macrophage-stimulating protein receptor;
Short=MSP receptor;
EC=2.7.10.1;
AltName: Full=CDw136;
AltName: Full=Protein-tyrosine kinase 8;
AltName: Full=p185-Ron;
AltName: CD_antigen=CD136;
Contains:
RecName: Full=Macrophage-stimulating protein receptor alpha chain;
Contains:
RecName: Full=Macrophage-stimulating protein receptor beta chain;
Flags: Precursor;
Name=MST1R; Synonyms=PTK8, RON;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RON), AND VARIANTS GLN-322;
ARG-523 AND GLY-1195.
TISSUE=Keratinocyte;
PubMed=8386824;
Ronsin C., Muscatelli F., Mattei M.-G., Breathnach R.;
"A novel putative receptor protein tyrosine kinase of the met
family.";
Oncogene 8:1195-1202(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=8816464; DOI=10.1128/MCB.16.10.5518;
Collesi C., Santoro M.M., Gaudino G., Comoglio P.M.;
"A splicing variant of the RON transcript induces constitutive
tyrosine kinase activity and an invasive phenotype.";
Mol. Cell. Biol. 16:5518-5526(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RON-1; RON-2; RON-3 AND RON-4).
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
INTERACTION WITH PIK3R1.
PubMed=7687741; DOI=10.1128/MCB.13.8.4600;
Ponzetto C., Bardelli A., Maina F., Longati P., Panayotou G.,
Dhand R., Waterfield M.D., Comoglio P.M.;
"A novel recognition motif for phosphatidylinositol 3-kinase binding
mediates its association with the hepatocyte growth factor/scatter
factor receptor.";
Mol. Cell. Biol. 13:4600-4608(1993).
[6]
TISSUE SPECIFICITY.
PubMed=8062829;
Gaudino G., Follenzi A., Naldini L., Collesi C., Santoro M.,
Gallo K.A., Godowski P.J., Comoglio P.M.;
"RON is a heterodimeric tyrosine kinase receptor activated by the HGF
homologue MSP.";
EMBO J. 13:3524-3532(1994).
[7]
FUNCTION.
PubMed=7939629; DOI=10.1126/science.7939629;
Wang M.-H., Ronsin C., Gesnel M.-C., Coupey L., Skeel A.,
Leonard E.J., Breatnach R.;
"Identification of the ron gene product as the receptor for the human
macrophage stimulating protein.";
Science 266:117-119(1994).
[8]
FUNCTION IN WOUND HEALING RESPONSE.
PubMed=9764835; DOI=10.1046/j.1523-1747.1998.00332.x;
Nanney L.B., Skeel A., Luan J., Polis S., Richmond A., Wang M.H.,
Leonard E.J.;
"Proteolytic cleavage and activation of pro-macrophage-stimulating
protein and upregulation of its receptor in tissue injury.";
J. Invest. Dermatol. 111:573-581(1998).
[9]
INTERACTION WITH ITGB1.
PubMed=10222149; DOI=10.1006/excr.1999.4429;
Danilkovitch A., Skeel A., Leonard E.J.;
"Macrophage stimulating protein-induced epithelial cell adhesion is
mediated by a PI3-K-dependent, but FAK-independent mechanism.";
Exp. Cell Res. 248:575-582(1999).
[10]
INTERACTION WITH MST1.
PubMed=10514476; DOI=10.1074/jbc.274.42.29937;
Danilkovitch A., Miller M., Leonard E.J.;
"Interaction of macrophage-stimulating protein with its receptor.
Residues critical for beta chain binding and evidence for independent
alpha chain binding.";
J. Biol. Chem. 274:29937-29943(1999).
[11]
REVIEW ON FUNCTION.
PubMed=12472665; DOI=10.1046/j.1365-3083.2002.01177.x;
Wang M.H., Zhou Y.Q., Chen Y.Q.;
"Macrophage-stimulating protein and RON receptor tyrosine kinase:
potential regulators of macrophage inflammatory activities.";
Scand. J. Immunol. 56:545-553(2002).
[12]
UBIQUITINATION.
PubMed=12802274; DOI=10.1038/sj.onc.1206585;
Penengo L., Rubin C., Yarden Y., Gaudino G.;
"c-Cbl is a critical modulator of the Ron tyrosine kinase receptor.";
Oncogene 22:3669-3679(2003).
[13]
INTERACTION WITH HYAL2.
PubMed=12676986; DOI=10.1073/pnas.0837136100;
Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D.,
Liu S.-L., Miller A.D., Lerman M.I.;
"Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and
mediates transformation of epithelial cells by jaagsiekte sheep
retrovirus.";
Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003).
[14]
INTERACTION WITH PLXNB1.
PubMed=15184888; DOI=10.1038/sj.onc.1207650;
Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.;
"Interplay between scatter factor receptors and B plexins controls
invasive growth.";
Oncogene 23:5131-5137(2004).
[15]
PHOSPHORYLATION AT TYR-1238; TYR-1239; TYR-1353 AND TYR-1360, AND
ENZYME REGULATION.
PubMed=15632155; DOI=10.1074/jbc.M412623200;
Yokoyama N., Ischenko I., Hayman M.J., Miller W.T.;
"The C terminus of RON tyrosine kinase plays an autoinhibitory role.";
J. Biol. Chem. 280:8893-8900(2005).
[16]
FUNCTION.
PubMed=18836480; DOI=10.1038/onc.2008.383;
Feres K.J., Ischenko I., Hayman M.J.;
"The RON receptor tyrosine kinase promotes MSP-independent cell
spreading and survival in breast epithelial cells.";
Oncogene 28:279-288(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INTERACTION WITH GAB1 AND GRB2.
PubMed=21784853; DOI=10.1074/jbc.M111.239384;
Chaudhuri A., Xie M.H., Yang B., Mahapatra K., Liu J., Marsters S.,
Bodepudi S., Ashkenazi A.;
"Distinct involvement of the Gab1 and Grb2 adaptor proteins in signal
transduction by the related receptor tyrosine kinases RON and MET.";
J. Biol. Chem. 286:32762-32774(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1060-1357 IN COMPLEX WITH
AMP-PNP AND MAGNESIUM, ACTIVE SITE, AND PHOSPHORYLATION AT TYR-1238.
PubMed=20726546; DOI=10.1021/bi100409w;
Wang J., Steinbacher S., Augustin M., Schreiner P., Epstein D.,
Mulvihill M.J., Crew A.P.;
"The crystal structure of a constitutively active mutant RON kinase
suggests an intramolecular autophosphorylation hypothesis.";
Biochemistry 49:7972-7974(2010).
[20]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 42-568, GLYCOSYLATION AT
ASN-488, AND DISULFIDE BONDS.
PubMed=22848655; DOI=10.1371/journal.pone.0041912;
Chao K.L., Tsai I.W., Chen C., Herzberg O.;
"Crystal structure of the Sema-PSI extracellular domain of human RON
receptor tyrosine kinase.";
PLoS ONE 7:E41912-E41912(2012).
[21]
VARIANTS [LARGE SCALE ANALYSIS] SER-75; THR-95; CYS-185; GLN-322;
ASP-356; LEU-434; ASP-465; CYS-504; ARG-523; PRO-613; MET-900;
GLY-1304; GLY-1335 AND CYS-1360.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[22]
VARIANTS NPCA3 HIS-306; THR-327; GLY-670 AND THR-973, AND INVOLVEMENT
IN NPCA3.
PubMed=26951679; DOI=10.1073/pnas.1523436113;
Dai W., Zheng H., Cheung A.K., Tang C.S., Ko J.M., Wong B.W.,
Leong M.M., Sham P.C., Cheung F., Kwong D.L., Ngan R.K., Ng W.T.,
Yau C.C., Pan J., Peng X., Tung S., Zhang Z., Ji M., Chiang A.K.,
Lee A.W., Lee V.H., Lam K.O., Au K.H., Cheng H.C., Yiu H.H.,
Lung M.L.;
"Whole-exome sequencing identifies MST1R as a genetic susceptibility
gene in nasopharyngeal carcinoma.";
Proc. Natl. Acad. Sci. U.S.A. 113:3317-3322(2016).
-!- FUNCTION: Receptor tyrosine kinase that transduces signals from
the extracellular matrix into the cytoplasm by binding to MST1
ligand. Regulates many physiological processes including cell
survival, migration and differentiation. Ligand binding at the
cell surface induces autophosphorylation of RON on its
intracellular domain that provides docking sites for downstream
signaling molecules. Following activation by ligand, interacts
with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1.
Recruitment of these downstream effectors by RON leads to the
activation of several signaling cascades including the RAS-ERK,
PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound
healing response by promoting epithelial cell migration,
proliferation as well as survival at the wound site. Plays also a
role in the innate immune response by regulating the migration and
phagocytic activity of macrophages. Alternatively, RON can also
promote signals such as cell migration and proliferation in
response to growth factors other than MST1 ligand.
{ECO:0000269|PubMed:18836480, ECO:0000269|PubMed:7939629,
ECO:0000269|PubMed:9764835}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: In its inactive state, the C-terminal tail
interacts with the catalytic domain and inhibits the kinase
activity. Upon ligand binding, the C-terminal tail is displaced
and becomes phosphorylated, thus increasing the kinase activity.
{ECO:0000269|PubMed:15632155}.
-!- SUBUNIT: Heterodimer of an alpha chain and a beta chain which are
disulfide linked. Binds PLXNB1. Associates with and is negatively
regulated by HYAL2. Interacts when phosphorylated with downstream
effectors including PIK3R1, PCLG1, GRB2 and GAB1. Interacts with
integrin beta1/ITGB1 in a ligand-independent fashion.
{ECO:0000269|PubMed:10222149, ECO:0000269|PubMed:10514476,
ECO:0000269|PubMed:12676986, ECO:0000269|PubMed:15184888,
ECO:0000269|PubMed:20726546, ECO:0000269|PubMed:21784853,
ECO:0000269|PubMed:7687741}.
-!- INTERACTION:
P26927:MST1; NbExp=5; IntAct=EBI-2637518, EBI-6929133;
O43157:PLXNB1; NbExp=3; IntAct=EBI-2637518, EBI-1111488;
O15031:PLXNB2; NbExp=2; IntAct=EBI-2637518, EBI-722004;
Q9ULL4:PLXNB3; NbExp=2; IntAct=EBI-2637518, EBI-311073;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=RON;
IsoId=Q04912-1; Sequence=Displayed;
Name=Delta-RON; Synonyms=sf-RON;
IsoId=Q04912-2; Sequence=VSP_005007;
Note=Lacks part of the extracellular domain, oligomerizes and is
constitutively activated. Expressed at higher level in cancer
cells. {ECO:0000303|PubMed:26951679};
Name=RON-1;
IsoId=Q04912-3; Sequence=VSP_038920, VSP_038921;
Name=RON-2;
IsoId=Q04912-4; Sequence=VSP_038919, VSP_038922, VSP_038923;
Name=RON-3;
IsoId=Q04912-5; Sequence=VSP_038924, VSP_038925;
Name=RON-4;
IsoId=Q04912-6; Sequence=VSP_038922, VSP_038923;
-!- TISSUE SPECIFICITY: Expressed in colon, skin, lung and bone
marrow. {ECO:0000269|PubMed:8062829}.
-!- PTM: Proteolytic processing yields the two subunits.
-!- PTM: Autophosphorylated in response to ligand binding on Tyr-1238
and Tyr-1239 in the kinase domain leading to further
phosphorylation of Tyr-1353 and Tyr-1360 in the C-terminal
multifunctional docking site. {ECO:0000269|PubMed:15632155,
ECO:0000269|PubMed:20726546}.
-!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
stability and activity through proteasomal degradation.
{ECO:0000269|PubMed:12802274}.
-!- DISEASE: Nasopharyngeal carcinoma, 3 (NPCA3) [MIM:617075]: A form
of nasopharyngeal carcinoma, a malignant neoplasm that originates
in the nasopharyngeal epithelium and includes 4 subtypes:
keratinizing squamous cell, non-keratinizing, basaloid squamous
cell, and papillary adenocarcinoma. {ECO:0000269|PubMed:26951679}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RONID287.html";
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EMBL; X70040; CAA49634.1; -; mRNA.
EMBL; EU826582; ACF47618.1; -; mRNA.
EMBL; EU826583; ACF47619.1; -; mRNA.
EMBL; EU826584; ACF47620.1; -; mRNA.
EMBL; EU826585; ACF47621.1; -; mRNA.
EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS2807.1; -. [Q04912-1]
CCDS; CCDS58833.1; -. [Q04912-2]
PIR; I38185; I38185.
RefSeq; NP_001231866.1; NM_001244937.2.
RefSeq; NP_002438.2; NM_002447.3.
UniGene; Hs.517973; -.
PDB; 3PLS; X-ray; 2.24 A; A=1060-1357.
PDB; 4FWW; X-ray; 1.85 A; A=42-568.
PDB; 4QT8; X-ray; 3.00 A; A/B=25-683.
PDBsum; 3PLS; -.
PDBsum; 4FWW; -.
PDBsum; 4QT8; -.
ProteinModelPortal; Q04912; -.
SMR; Q04912; -.
BioGrid; 110592; 24.
DIP; DIP-6029N; -.
IntAct; Q04912; 15.
MINT; MINT-6539690; -.
STRING; 9606.ENSP00000296474; -.
BindingDB; Q04912; -.
ChEMBL; CHEMBL2689; -.
GuidetoPHARMACOLOGY; 1816; -.
iPTMnet; Q04912; -.
PhosphoSitePlus; Q04912; -.
BioMuta; MST1R; -.
DMDM; 294862462; -.
MaxQB; Q04912; -.
PaxDb; Q04912; -.
PeptideAtlas; Q04912; -.
PRIDE; Q04912; -.
DNASU; 4486; -.
Ensembl; ENST00000296474; ENSP00000296474; ENSG00000164078.
Ensembl; ENST00000344206; ENSP00000341325; ENSG00000164078.
GeneID; 4486; -.
KEGG; hsa:4486; -.
UCSC; uc003cxy.5; human. [Q04912-1]
CTD; 4486; -.
DisGeNET; 4486; -.
EuPathDB; HostDB:ENSG00000164078.12; -.
GeneCards; MST1R; -.
HGNC; HGNC:7381; MST1R.
HPA; CAB008972; -.
HPA; HPA007657; -.
HPA; HPA008180; -.
MalaCards; MST1R; -.
MIM; 255995; phenotype.
MIM; 600168; gene.
MIM; 617075; phenotype.
neXtProt; NX_Q04912; -.
PharmGKB; PA31186; -.
eggNOG; KOG1095; Eukaryota.
eggNOG; KOG3610; Eukaryota.
eggNOG; ENOG410XRIK; LUCA.
HOGENOM; HOG000220900; -.
HOVERGEN; HBG104342; -.
InParanoid; Q04912; -.
KO; K05100; -.
OrthoDB; EOG091G0751; -.
PhylomeDB; Q04912; -.
TreeFam; TF317402; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-8852405; Signaling by MST1.
SignaLink; Q04912; -.
SIGNOR; Q04912; -.
ChiTaRS; MST1R; human.
GeneWiki; MST1R; -.
GenomeRNAi; 4486; -.
PRO; PR:Q04912; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000164078; -.
CleanEx; HS_MST1R; -.
ExpressionAtlas; Q04912; baseline and differential.
Genevisible; Q04912; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0005773; C:vacuole; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; TAS:ProtInc.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007338; P:single fertilization; TAS:ProtInc.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016201; PSI.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01403; Sema; 1.
Pfam; PF01833; TIG; 3.
PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00429; IPT; 3.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF81296; SSF81296; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding;
Cleavage on pair of basic residues; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Immunity;
Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1400 Macrophage-stimulating protein receptor.
/FTId=PRO_0000024452.
CHAIN 25 304 Macrophage-stimulating protein receptor
alpha chain. {ECO:0000255}.
/FTId=PRO_0000024453.
CHAIN 310 1400 Macrophage-stimulating protein receptor
beta chain. {ECO:0000255}.
/FTId=PRO_0000024454.
TOPO_DOM 25 957 Extracellular. {ECO:0000255}.
TRANSMEM 958 978 Helical. {ECO:0000255}.
TOPO_DOM 979 1400 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 522 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 569 671 IPT/TIG 1.
DOMAIN 684 767 IPT/TIG 2.
DOMAIN 770 860 IPT/TIG 3.
DOMAIN 1082 1345 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1088 1096 ATP.
NP_BIND 1161 1164 ATP.
COMPBIAS 306 309 Poly-Arg.
COMPBIAS 962 968 Poly-Leu.
ACT_SITE 1208 1208 Proton acceptor.
{ECO:0000305|PubMed:20726546}.
BINDING 1114 1114 ATP.
BINDING 1212 1212 ATP.
MOD_RES 1238 1238 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:15632155,
ECO:0000305|PubMed:20726546}.
MOD_RES 1239 1239 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:15632155}.
MOD_RES 1353 1353 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15632155}.
MOD_RES 1360 1360 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15632155}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 419 419 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22848655}.
CARBOHYD 654 654 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 841 841 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 897 897 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 101 104 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 107 162 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 135 143 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 174 177 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 300 367 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 385 407 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 386 422 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 527 545 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 533 567 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 536 552 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
DISULFID 548 558 {ECO:0000255|PROSITE-ProRule:PRU00352,
ECO:0000269|PubMed:22848655}.
VAR_SEQ 411 516 Missing (in isoform RON-2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_038919.
VAR_SEQ 475 495 ELVRSLNYLLYVSNFSLGDSG -> GPHPHSPLALGPCLHP
HFAHI (in isoform RON-1).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_038920.
VAR_SEQ 496 1400 Missing (in isoform RON-1).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_038921.
VAR_SEQ 628 647 PVPRKDFVEEFECELEPLGT -> YNLVPPLPFPEGGNQAA
PSP (in isoform RON-2 and isoform RON-4).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_038922.
VAR_SEQ 648 1400 Missing (in isoform RON-2 and isoform
RON-4). {ECO:0000303|PubMed:18593464}.
/FTId=VSP_038923.
VAR_SEQ 884 932 Missing (in isoform Delta-RON).
{ECO:0000305}.
/FTId=VSP_005007.
VAR_SEQ 884 907 YIGLGAVADCVGINVTVGGESCQH -> VSVRDRGRDSWGS
ESRGQPTGWSS (in isoform RON-3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_038924.
VAR_SEQ 908 1400 Missing (in isoform RON-3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_038925.
VARIANT 75 75 R -> S (in dbSNP:rs35887539).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041768.
VARIANT 95 95 P -> T (in dbSNP:rs55908300).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041769.
VARIANT 185 185 R -> C (in dbSNP:rs55633379).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041770.
VARIANT 306 306 R -> H (in NPCA3).
{ECO:0000269|PubMed:26951679}.
/FTId=VAR_076928.
VARIANT 322 322 R -> Q (in dbSNP:rs2230593).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8386824}.
/FTId=VAR_006350.
VARIANT 327 327 A -> T (in NPCA3; unknown pathological
significance).
{ECO:0000269|PubMed:26951679}.
/FTId=VAR_076929.
VARIANT 356 356 G -> D (in dbSNP:rs35924402).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041771.
VARIANT 434 434 S -> L (in dbSNP:rs2230591).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_029238.
VARIANT 440 440 N -> S (in dbSNP:rs2230592).
/FTId=VAR_029239.
VARIANT 465 465 G -> D (in dbSNP:rs34564898).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041772.
VARIANT 504 504 R -> C (in dbSNP:rs34350470).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041773.
VARIANT 523 523 Q -> R (in dbSNP:rs2230590).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8386824}.
/FTId=VAR_041774.
VARIANT 613 613 Q -> P (in dbSNP:rs35986685).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041775.
VARIANT 670 670 V -> G (in NPCA3; unknown pathological
significance).
{ECO:0000269|PubMed:26951679}.
/FTId=VAR_076930.
VARIANT 900 900 V -> M (in dbSNP:rs56091918).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041776.
VARIANT 973 973 A -> T (in NPCA3; unknown pathological
significance).
{ECO:0000269|PubMed:26951679}.
/FTId=VAR_076931.
VARIANT 1195 1195 S -> G (in dbSNP:rs7433231).
{ECO:0000269|PubMed:8386824}.
/FTId=VAR_061749.
VARIANT 1304 1304 R -> G. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041777.
VARIANT 1335 1335 R -> G (in dbSNP:rs1062633).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_024577.
VARIANT 1360 1360 Y -> C (in dbSNP:rs56330223).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041778.
CONFLICT 209 209 A -> G (in Ref. 1; CAA49634).
{ECO:0000305}.
CONFLICT 813 813 R -> RQ (in Ref. 3; ACF47620).
{ECO:0000305}.
STRAND 43 45 {ECO:0000244|PDB:4FWW}.
STRAND 48 50 {ECO:0000244|PDB:4FWW}.
STRAND 55 62 {ECO:0000244|PDB:4FWW}.
STRAND 64 66 {ECO:0000244|PDB:4QT8}.
STRAND 68 74 {ECO:0000244|PDB:4FWW}.
STRAND 77 81 {ECO:0000244|PDB:4FWW}.
STRAND 87 92 {ECO:0000244|PDB:4FWW}.
STRAND 96 98 {ECO:0000244|PDB:4QT8}.
HELIX 102 105 {ECO:0000244|PDB:4FWW}.
STRAND 108 110 {ECO:0000244|PDB:4FWW}.
STRAND 120 126 {ECO:0000244|PDB:4FWW}.
TURN 127 130 {ECO:0000244|PDB:4FWW}.
STRAND 131 138 {ECO:0000244|PDB:4FWW}.
HELIX 139 141 {ECO:0000244|PDB:4FWW}.
STRAND 143 151 {ECO:0000244|PDB:4FWW}.
STRAND 154 157 {ECO:0000244|PDB:4FWW}.
STRAND 161 163 {ECO:0000244|PDB:4QT8}.
TURN 166 168 {ECO:0000244|PDB:4QT8}.
STRAND 184 191 {ECO:0000244|PDB:4FWW}.
STRAND 194 201 {ECO:0000244|PDB:4FWW}.
HELIX 205 208 {ECO:0000244|PDB:4FWW}.
STRAND 209 211 {ECO:0000244|PDB:4FWW}.
STRAND 215 221 {ECO:0000244|PDB:4FWW}.
STRAND 233 235 {ECO:0000244|PDB:4FWW}.
HELIX 239 242 {ECO:0000244|PDB:4FWW}.
STRAND 248 255 {ECO:0000244|PDB:4FWW}.
STRAND 258 268 {ECO:0000244|PDB:4FWW}.
STRAND 269 271 {ECO:0000244|PDB:4QT8}.
STRAND 275 288 {ECO:0000244|PDB:4FWW}.
HELIX 290 292 {ECO:0000244|PDB:4QT8}.
STRAND 294 302 {ECO:0000244|PDB:4FWW}.
STRAND 309 311 {ECO:0000244|PDB:4QT8}.
STRAND 316 318 {ECO:0000244|PDB:4FWW}.
STRAND 320 328 {ECO:0000244|PDB:4FWW}.
HELIX 331 337 {ECO:0000244|PDB:4FWW}.
STRAND 344 351 {ECO:0000244|PDB:4FWW}.
STRAND 365 370 {ECO:0000244|PDB:4FWW}.
HELIX 371 386 {ECO:0000244|PDB:4FWW}.
STRAND 387 389 {ECO:0000244|PDB:4FWW}.
TURN 399 401 {ECO:0000244|PDB:4FWW}.
STRAND 407 409 {ECO:0000244|PDB:4QT8}.
HELIX 422 424 {ECO:0000244|PDB:4FWW}.
STRAND 433 436 {ECO:0000244|PDB:4FWW}.
TURN 438 445 {ECO:0000244|PDB:4FWW}.
STRAND 448 456 {ECO:0000244|PDB:4FWW}.
STRAND 459 466 {ECO:0000244|PDB:4FWW}.
STRAND 469 475 {ECO:0000244|PDB:4FWW}.
STRAND 485 491 {ECO:0000244|PDB:4FWW}.
STRAND 503 505 {ECO:0000244|PDB:4FWW}.
STRAND 508 513 {ECO:0000244|PDB:4FWW}.
STRAND 516 521 {ECO:0000244|PDB:4FWW}.
HELIX 527 529 {ECO:0000244|PDB:4FWW}.
HELIX 533 538 {ECO:0000244|PDB:4FWW}.
HELIX 541 543 {ECO:0000244|PDB:4FWW}.
STRAND 549 553 {ECO:0000244|PDB:4FWW}.
HELIX 555 557 {ECO:0000244|PDB:4FWW}.
TURN 559 561 {ECO:0000244|PDB:4FWW}.
STRAND 563 567 {ECO:0000244|PDB:4QT8}.
STRAND 570 575 {ECO:0000244|PDB:4QT8}.
STRAND 578 580 {ECO:0000244|PDB:4QT8}.
STRAND 589 593 {ECO:0000244|PDB:4QT8}.
STRAND 609 615 {ECO:0000244|PDB:4QT8}.
STRAND 639 641 {ECO:0000244|PDB:4QT8}.
STRAND 653 659 {ECO:0000244|PDB:4QT8}.
STRAND 672 682 {ECO:0000244|PDB:4QT8}.
HELIX 1064 1069 {ECO:0000244|PDB:3PLS}.
HELIX 1071 1073 {ECO:0000244|PDB:3PLS}.
HELIX 1077 1079 {ECO:0000244|PDB:3PLS}.
STRAND 1080 1091 {ECO:0000244|PDB:3PLS}.
STRAND 1094 1102 {ECO:0000244|PDB:3PLS}.
STRAND 1104 1106 {ECO:0000244|PDB:3PLS}.
STRAND 1108 1116 {ECO:0000244|PDB:3PLS}.
HELIX 1122 1136 {ECO:0000244|PDB:3PLS}.
STRAND 1148 1150 {ECO:0000244|PDB:3PLS}.
STRAND 1153 1155 {ECO:0000244|PDB:3PLS}.
STRAND 1158 1161 {ECO:0000244|PDB:3PLS}.
HELIX 1169 1174 {ECO:0000244|PDB:3PLS}.
HELIX 1182 1201 {ECO:0000244|PDB:3PLS}.
HELIX 1211 1213 {ECO:0000244|PDB:3PLS}.
STRAND 1214 1216 {ECO:0000244|PDB:3PLS}.
STRAND 1222 1224 {ECO:0000244|PDB:3PLS}.
TURN 1232 1235 {ECO:0000244|PDB:3PLS}.
HELIX 1236 1239 {ECO:0000244|PDB:3PLS}.
HELIX 1250 1253 {ECO:0000244|PDB:3PLS}.
HELIX 1256 1259 {ECO:0000244|PDB:3PLS}.
HELIX 1266 1282 {ECO:0000244|PDB:3PLS}.
TURN 1287 1290 {ECO:0000244|PDB:3PLS}.
HELIX 1293 1295 {ECO:0000244|PDB:3PLS}.
HELIX 1296 1301 {ECO:0000244|PDB:3PLS}.
HELIX 1314 1323 {ECO:0000244|PDB:3PLS}.
HELIX 1328 1330 {ECO:0000244|PDB:3PLS}.
HELIX 1334 1347 {ECO:0000244|PDB:3PLS}.
SEQUENCE 1400 AA; 152271 MW; EB5CA79ABC69A882 CRC64;
MELLPPLPQS FLLLLLLPAK PAAGEDWQCP RTPYAASRDF DVKYVVPSFS AGGLVQAMVT
YEGDRNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPPGDTDT
KVLVLDPALP ALVSCGSSLQ GRCFLHDLEP QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS
PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK
HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DDPSALHTRL ARLSATEPEL GDYRELVLDC
RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VTGKDGGPGV
GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEALSPNT
SCRHFPLLVS SSFSRVDLFN GLLGPVQVTA LYVTRLDNVT VAHMGTMDGR ILQVELVRSL
NYLLYVSNFS LGDSGQPVQR DVSRLGDHLL FASGDQVFQV PIQGPGCRHF LTCGRCLRAW
HFMGCGWCGN MCGQQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG
LVPEGTHQVT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV GPTNVSLTVT
NMPPGKHFRV DGTSVLRGFS FMEPVLIAVQ PLFGPRAGGT CLTLEGQSLS VGTSRAVLVN
GTECLLARVS EGQLLCATPP GATVASVPLS LQVGGAQVPG SWTFQYREDP VVLSISPNCG
YINSHITICG QHLTSAWHLV LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VRDPQGWVAG
NLSARGDGAA GFTLPGFRFL PPPHPPSANL VPLKPEEHAI KFEYIGLGAV ADCVGINVTV
GGESCQHEFR GDMVVCPLPP SLQLGQDGAP LQVCVDGECH ILGRVVRPGP DGVPQSTLLG
ILLPLLLLVA ALATALVFSY WWRRKQLVLP PNLNDLASLD QTAGATPLPI LYSGSDYRSG
LALPAIDGLD STTCVHGASF SDSEDESCVP LLRKESIQLR DLDSALLAEV KDVLIPHERV
VTHSDRVIGK GHFGVVYHGE YIDQAQNRIQ CAIKSLSRIT EMQQVEAFLR EGLLMRGLNH
PNVLALIGIM LPPEGLPHVL LPYMCHGDLL QFIRSPQRNP TVKDLISFGL QVARSMEYLA
EQKFVHRDLA ARNCMLDESF TVKVADFGLA RDILDREYYS VQQHRHARLP VKWMALESLQ
TYRFTTKSDV WSFGVLLWEL LTRGAPPYRH IDPFDLTHFL AQGRRLPQPE YCPDSLYQVM
QQCWEADPAV RPTFRVLVGE VEQIVSALLG DHYVQLPATY MNLGPSTSHE MNVRPEQPQF
SPMPGNVRRP RPLSEPPRPT


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