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Fibroblast growth factor receptor 3 (FGFR-3) (EC 2.7.10.1) (Heparin-binding growth factor receptor) (CD antigen CD333)

 FGFR3_MOUSE             Reviewed;         801 AA.
Q61851; Q61564; Q63834;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 162.
RecName: Full=Fibroblast growth factor receptor 3;
Short=FGFR-3;
EC=2.7.10.1;
AltName: Full=Heparin-binding growth factor receptor;
AltName: CD_antigen=CD333;
Flags: Precursor;
Name=Fgfr3; Synonyms=Mfr3, Sam3;
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).
PubMed=1379594;
Ornitz D.M., Leder P.;
"Ligand specificity and heparin dependence of fibroblast growth factor
receptors 1 and 3.";
J. Biol. Chem. 267:16305-16311(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8382556;
Katoh O., Hattori Y., Sasaki H., Sakamoto H., Fujimoto K., Fujii T.,
Sugimura T., Terada M.;
"Isolation of the complementary DNA encoding a mouse heparin-binding
growth factor receptor with the use of a unique kinase insert
sequence.";
Cancer Res. 53:1136-1141(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-364 (ISOFORM 2).
PubMed=7512569;
Chellaiah A.T., McEwen D.G., Werner S., Xu J., Ornitz D.M.;
"Fibroblast growth factor receptor (FGFR) 3. Alternative splicing in
immunoglobulin-like domain III creates a receptor highly specific for
acidic FGF/FGF-1.";
J. Biol. Chem. 269:11620-11627(1994).
[4]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=8601314; DOI=10.1016/S0092-8674(00)81069-7;
Deng C., Wynshaw-Boris A., Zhou F., Kuo A., Leder P.;
"Fibroblast growth factor receptor 3 is a negative regulator of bone
growth.";
Cell 84:911-921(1996).
[5]
INTERACTION WITH FGF1; FGF2; FGF4; FGF8 AND FGF9, AND FUNCTION IN CELL
PROLIFERATION.
PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
Coulier F., Gao G., Goldfarb M.;
"Receptor specificity of the fibroblast growth factor family.";
J. Biol. Chem. 271:15292-15297(1996).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=8630492; DOI=10.1038/ng0496-390;
Colvin J.S., Bohne B.A., Harding G.W., McEwen D.G., Ornitz D.M.;
"Skeletal overgrowth and deafness in mice lacking fibroblast growth
factor receptor 3.";
Nat. Genet. 12:390-397(1996).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9716527;
Weinstein M., Xu X., Ohyama K., Deng C.X.;
"FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in
the murine lung.";
Development 125:3615-3623(1998).
[8]
FUNCTION AS FGF2 RECEPTOR AND IN PHOSPHORYLATION OF CBL,
UBIQUITINATION, PHOSPHORYLATION, ENZYME REGULATION, AND MUTAGENESIS OF
644.
PubMed=14699054; DOI=10.1073/pnas.2237184100;
Cho J.Y., Guo C., Torello M., Lunstrum G.P., Iwata T., Deng C.,
Horton W.A.;
"Defective lysosomal targeting of activated fibroblast growth factor
receptor 3 in achondroplasia.";
Proc. Natl. Acad. Sci. U.S.A. 101:609-614(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-439, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION IN VITAMIN D METABOLISM.
PubMed=21561999; DOI=10.1152/ajprenal.00740.2010;
Gattineni J., Twombley K., Goetz R., Mohammadi M., Baum M.;
"Regulation of serum 1,25(OH)2Vitamin D3 levels by fibroblast growth
factor 23 is mediated by FGF receptors 3 and 4.";
Am. J. Physiol. 301:F371-F377(2011).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for fibroblast growth factors and plays an essential role
in the regulation of cell proliferation, differentiation and
apoptosis. Plays an essential role in the regulation of
chondrocyte differentiation, proliferation and apoptosis, and is
required for normal skeleton development. Regulates both
osteogenesis and postnatal bone mineralization by osteoblasts.
Promotes apoptosis in chondrocytes, but can also promote cancer
cell proliferation. Required for normal development of the inner
ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to
the activation of several signaling cascades. Activation of PLCG1
leads to the production of the cellular signaling molecules
diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation
of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and
mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP
kinase signaling pathway, as well as of the AKT1 signaling
pathway. Plays a role in the regulation of vitamin D metabolism.
Mutations that lead to constitutive kinase activation or impair
normal FGFR3 maturation, internalization and degradation lead to
aberrant signaling. Over-expressed or constitutively activated
FGFR3 promotes activation of STAT1, STAT5A and STAT5B. Plays a
role in postnatal lung development. {ECO:0000269|PubMed:14699054,
ECO:0000269|PubMed:21561999, ECO:0000269|PubMed:8601314,
ECO:0000269|PubMed:8630492, ECO:0000269|PubMed:8663044,
ECO:0000269|PubMed:9716527}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Ligand binding leads to dimerization and
activation by autophosphorylation on tyrosine residues (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts with
FGF1, FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19,
FGF20 and FGF23 (in vitro). Interacts with KLB. Affinity for
fibroblast growth factors (FGFs) is increased by heparan sulfate
glycosaminoglycans that function as coreceptors. Likewise, KLB
increases the affinity for FGF19 and FGF21. Interacts with PIK3R1,
PLCG1, SOCS1 and SOCS3 (By similarity). {ECO:0000250}.
-!- INTERACTION:
O35082:Kl; NbExp=2; IntAct=EBI-15820536, EBI-1570828;
Q9JID9:Sh2b2; NbExp=3; IntAct=EBI-6287052, EBI-8100899;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum
{ECO:0000250}. Note=The activated receptor is rapidly internalized
and degraded. Detected in intracellular vesicles after
internalization of the autophosphorylated receptor (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=IIIc;
IsoId=Q61851-1; Sequence=Displayed;
Name=2; Synonyms=IIIb;
IsoId=Q61851-2; Sequence=VSP_002990;
-!- TISSUE SPECIFICITY: In embryo, expressed in heart, lung, kidney,
skin, head and liver but not in muscle. In adult, highest levels
in brain. Also expressed in liver, lung, kidney, testis, ovary and
uterus. Very low levels in heart, thymus, spleen and muscle.
-!- DEVELOPMENTAL STAGE: Expressed in embryos from mid-gestation and
in adult.
-!- DOMAIN: The second and third Ig-like domains directly interact
with fibroblast growth factors (FGF) and heparan sulfate
proteoglycans. {ECO:0000250}.
-!- PTM: Autophosphorylated. Binding of FGF family members together
with heparan sulfate proteoglycan or heparin promotes receptor
dimerization and autophosphorylation on tyrosine residues.
Autophosphorylation occurs in trans between the two FGFR molecules
present in the dimer. Phosphorylation at Tyr-719 is essential for
stimulation of cell proliferation and activation of PIK3R1, STAT1
and MAP kinase signaling. Phosphorylation at Tyr-755 is required
for interaction with PIK3R1 and PLCG1 (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated. Is rapidly ubiquitinated after ligand binding
and autophosphorylation, leading to receptor internalization and
degradation. Subject to both proteasomal and lysosomal degradation
(By similarity). {ECO:0000250}.
-!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan
chains undergo further maturation to an Endo H-resistant form in
the Golgi apparatus (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice exhibit defects in their skeleton,
including kyphosis, scoliosis, crooked tails and curvature and
overgrowth of long bones and vertebrae. This bone dysplasia is due
to defects in the regulation of chondrocyte proliferation and
differentiation in the cartilaginous growth plate. Mice also
display inner ear defects including failure of pillar cell
differentiation and tunnel of Corti formation, resulting in
profound deafness. Mice lacking both FGFR3 and FGFR4 display
pronounced dwarfism, and while their lungs appear normal at birth,
they are completely blocked in alveogenesis and do not form
secondary septae to delimit alveoli. These mice also show elevated
serum levels of 1,25-dihydroxyvitamin D3 and reduced serum
phosphorus levels. {ECO:0000269|PubMed:21561999,
ECO:0000269|PubMed:8601314, ECO:0000269|PubMed:8630492,
ECO:0000269|PubMed:9716527}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fibroblast growth factor receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; M81342; AAA39535.1; -; mRNA.
EMBL; S56291; AAB25535.1; -; mRNA.
EMBL; L26492; AAA21490.2; -; Genomic_DNA.
PIR; A48991; A48991.
PIR; I55363; I55363.
UniGene; Mm.6904; -.
ProteinModelPortal; Q61851; -.
SMR; Q61851; -.
DIP; DIP-6031N; -.
IntAct; Q61851; 4.
MINT; MINT-5181473; -.
STRING; 10090.ENSMUSP00000133064; -.
BindingDB; Q61851; -.
ChEMBL; CHEMBL4066; -.
iPTMnet; Q61851; -.
PhosphoSitePlus; Q61851; -.
PaxDb; Q61851; -.
PRIDE; Q61851; -.
MGI; MGI:95524; Fgfr3.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; Q61851; -.
PhylomeDB; Q61851; -.
BRENDA; 2.7.10.1; 3474.
ChiTaRS; Fgfr3; mouse.
PRO; PR:Q61851; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_FGFR3; -.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0030133; C:transport vesicle; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; IDA:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0061144; P:alveolar secondary septum development; IGI:MGI.
GO; GO:0060385; P:axonogenesis involved in innervation; IMP:MGI.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0070977; P:bone maturation; IMP:BHF-UCL.
GO; GO:0030282; P:bone mineralization; IMP:BHF-UCL.
GO; GO:0060349; P:bone morphogenesis; IMP:BHF-UCL.
GO; GO:0061430; P:bone trabecula morphogenesis; IMP:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
GO; GO:0090102; P:cochlea development; IMP:MGI.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
GO; GO:0072148; P:epithelial cell fate commitment; IMP:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:1902178; P:fibroblast growth factor receptor apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0060113; P:inner ear receptor cell differentiation; IMP:MGI.
GO; GO:0070307; P:lens fiber cell development; IGI:MGI.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0000165; P:MAPK cascade; IDA:MGI.
GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0048640; P:negative regulation of developmental growth; IMP:BHF-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0045839; P:negative regulation of mitotic nuclear division; IGI:MGI.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
GO; GO:0038066; P:p38MAPK cascade; IMP:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IMP:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0010518; P:positive regulation of phospholipase activity; ISS:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:0036342; P:post-anal tail morphogenesis; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0046850; P:regulation of bone remodeling; IMP:MGI.
GO; GO:0010712; P:regulation of collagen metabolic process; IMP:MGI.
GO; GO:0030278; P:regulation of ossification; IMP:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
GO; GO:0048678; P:response to axon injury; IMP:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
GO; GO:0021762; P:substantia nigra development; IMP:MGI.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR016248; FGF_rcpt_fam.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07679; I-set; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF000628; FGFR; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Immunoglobulin domain; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 801 Fibroblast growth factor receptor 3.
/FTId=PRO_0000016786.
TOPO_DOM 21 369 Extracellular. {ECO:0000255}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TOPO_DOM 391 801 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 124 Ig-like C2-type 1.
DOMAIN 145 238 Ig-like C2-type 2.
DOMAIN 247 349 Ig-like C2-type 3.
DOMAIN 466 756 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 472 480 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 611 611 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 502 502 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 641 641 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P22607}.
MOD_RES 642 642 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P22607}.
MOD_RES 719 719 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P22607}.
MOD_RES 755 755 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P22607}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 59 107 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 170 222 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 269 333 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 305 352 TAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHS
AWLVVLP -> SWISENVEADARLRLANVSERDGGEYLCRA
TNFIGVAEKAFWLRVHGPQA (in isoform 2).
{ECO:0000305}.
/FTId=VSP_002990.
MUTAGEN 644 644 K->E: Constitutively activated kinase.
{ECO:0000269|PubMed:14699054}.
CONFLICT 684 684 P -> L (in Ref. 2; AAB25535).
{ECO:0000305}.
CONFLICT 687 687 Missing (in Ref. 2; AAB25535).
{ECO:0000305}.
SEQUENCE 801 AA; 87758 MW; 68BC110212691705 CRC64;
MVVPACVLVF CVAVVAGATS EPPGPEQRVV RRAAEVPGPE PSQQEQVAFG SGDTVELSCH
PPGGAPTGPT VWAKDGTGLV ASHRILVGPQ RLQVLNASHE DAGVYSCQHR LTRRVLCHFS
VRVTDAPSSG DDEDGEDVAE DTGAPYWTRP ERMDKKLLAV PAANTVRFRC PAAGNPTPSI
SWLKNGKEFR GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKFGS IRQTYTLDVL
ERSPHRPILQ AGLPANQTAI LGSDVEFHCK VYSDAQPHIQ WLKHVEVNGS KVGPDGTPYV
TVLKTAGANT TDKELEVLSL HNVTFEDAGE YTCLAGNSIG FSHHSAWLVV LPAEEELMET
DEAGSVYAGV LSYGVVFFLF ILVVAAVILC RLRSPPKKGL GSPTVHKVSR FPLKRQVSLE
SNSSMNSNTP LVRIARLSSG EGPVLANVSE LELPADPKWE LSRTRLTLGK PLGEGCFGQV
VMAEAIGIDK DRTAKPVTVA VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT
QGGPLYVLVE YAAKGNLREF LRARRPPGMD YSFDACRLPE EQLTCKDLVS CAYQVARGME
YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNLD YYKKTTNGRL PVKWMAPEAL
FDRVYTHQSD VWSFGVLLWE IFTPGGPSPY PGIPVEELFK LLKEGHRMDK PASCTHDLYM
IMRECWHAVP SQRPTFKQLV EDLDRILTVT STDEYLDLSV PFEQYSPGGQ DTPSSSSSGD
DSVFTHDLLP PGPPSNGGPR T


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E0074h ELISA kit Basic fibroblast growth factor receptor 1,BFGFR,BFGFR,bFGF-R-1,CEK,FGFBR,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,FLG,FLT2,FLT-2,Fms-like tyrosine kinase 2,HBGFR,Homo sapiens,Human, 96T
E0074h ELISA Basic fibroblast growth factor receptor 1,BFGFR,BFGFR,bFGF-R-1,CEK,FGFBR,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,FLG,FLT2,FLT-2,Fms-like tyrosine kinase 2,HBGFR,Homo sapiens,Human,N-sam 96T
U0074c CLIA Basic fibroblast growth factor receptor 1,bFGF-R-1,CEK1,Chicken,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,Gallus gallus,Tyrosine kinase receptor CEK1 96T
E0074c ELISA Basic fibroblast growth factor receptor 1,bFGF-R-1,CEK1,Chicken,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,Gallus gallus,Tyrosine kinase receptor CEK1 96T
E0074c ELISA kit Basic fibroblast growth factor receptor 1,bFGF-R-1,CEK1,Chicken,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,Gallus gallus,Tyrosine kinase receptor CEK1 96T
E0034m ELISA kit Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
E0034m ELISA Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
U0034m CLIA Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
E0636h ELISA kit FGF7,FGF-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Homo sapiens,Human,Keratinocyte growth factor,KGF,KGF 96T
U0636h CLIA FGF7,FGF-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Homo sapiens,Human,Keratinocyte growth factor,KGF,KGF 96T
E0636h ELISA FGF7,FGF-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Homo sapiens,Human,Keratinocyte growth factor,KGF,KGF 96T
E0032p ELISA Acidic fibroblast growth factor,aFGF,Alpha-endothelial cell growth factor,FGF1,FGF-1,HBGF-1,Heparin-binding growth factor 1,Pig,Sus scrofa 96T
E0032p ELISA kit Acidic fibroblast growth factor,aFGF,Alpha-endothelial cell growth factor,FGF1,FGF-1,HBGF-1,Heparin-binding growth factor 1,Pig,Sus scrofa 96T
U0032p CLIA Acidic fibroblast growth factor,aFGF,Alpha-endothelial cell growth factor,FGF1,FGF-1,HBGF-1,Heparin-binding growth factor 1,Pig,Sus scrofa 96T
E0636r ELISA kit Fgf7,FGF-7,Fgf-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Keratinocyte growth factor,KGF,Kgf,Rat,Rattus norvegicus 96T
E0636m ELISA Fgf7,FGF-7,Fgf-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Keratinocyte growth factor,KGF,Mouse,Mus musculus 96T
E0636m ELISA kit Fgf7,FGF-7,Fgf-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Keratinocyte growth factor,KGF,Mouse,Mus musculus 96T


 

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