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Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331)

 FGFR1_RAT               Reviewed;         822 AA.
Q04589;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 157.
RecName: Full=Fibroblast growth factor receptor 1;
Short=FGFR-1;
Short=bFGF-R-1;
EC=2.7.10.1 {ECO:0000250|UniProtKB:P11362};
AltName: Full=Basic fibroblast growth factor receptor 1;
AltName: Full=MFR;
AltName: Full=Proto-oncogene c-Fgr;
AltName: CD_antigen=CD331;
Flags: Precursor;
Name=Fgfr1; Synonyms=Flg;
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].
PubMed=8382532; DOI=10.1016/0167-4781(93)90266-G;
Yazaki N., Hiroko F., Mitsuhiro O., Toshisuke K., Nobuyuki I.;
"The structure and expression of the FGF receptor-1 mRNA isoforms in
rat tissues.";
Biochim. Biophys. Acta 1172:37-42(1993).
[2]
INTERACTION WITH RPS6KA1, AND SUBCELLULAR LOCATION.
PubMed=15117958; DOI=10.1074/jbc.M311144200;
Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K.,
Stachowiak M.K.;
"90-kDa ribosomal S6 kinase is a direct target for the nuclear
fibroblast growth factor receptor 1 (FGFR1): role in FGFR1
signaling.";
J. Biol. Chem. 279:29325-29335(2004).
[3]
TISSUE SPECIFICITY.
PubMed=17992255; DOI=10.1172/JCI32409;
Ben-Dov I.Z., Galitzer H., Lavi-Moshayoff V., Goetz R., Kuro-o M.,
Mohammadi M., Sirkis R., Naveh-Many T., Silver J.;
"The parathyroid is a target organ for FGF23 in rats.";
J. Clin. Invest. 117:4003-4008(2007).
[4]
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: Tyrosine-protein kinase that acts as cell-surface
receptor for fibroblast growth factors and plays an essential role
in the regulation of embryonic development, cell proliferation,
differentiation and migration. Required for normal mesoderm
patterning and correct axial organization during embryonic
development, normal skeletogenesis and normal development of the
gonadotropin-releasing hormone (GnRH) neuronal system.
Phosphorylates PLCG1, FRS2, GAB1 and SHB. 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. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2.
In the nucleus, enhances RPS6KA1 and CREB1 activity and
contributes to the regulation of transcription. FGFR1 signaling is
down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination,
internalization and degradation (By similarity).
{ECO:0000250|UniProtKB:P11362, ECO:0000250|UniProtKB:P16092}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000250|UniProtKB:P11362,
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 sequential autophosphorylation on tyrosine residues
(By similarity). {ECO:0000250|UniProtKB:P11362}.
-!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts
predominantly with FGF1 and FGF2, but can also interact with FGF3,
FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in
vitro). Ligand specificity is determined by tissue-specific
expression of isoforms, and differences in the third Ig-like
domain are crucial for ligand specificity. Affinity for fibroblast
growth factors (FGFs) is increased by heparan sulfate
glycosaminoglycans that function as coreceptors. Likewise, KLB
increases the affinity for FGF19, FGF21 and FGF23. Interacts
(phosphorylated on Tyr-766) with PLCG1 (via SH2 domains).
Interacts with FRS2. Interacts (via C-terminus) with NEDD4 (via
WW3 domain). Interacts with RPS6KA1 (PubMed:15117958). Interacts
with KL (By similarity). Interacts with SHB (via SH2 domain) and
GRB10. Interacts with ANOS1; this interaction does not interfere
with FGF2-binding to FGFR1, but prevents binding of heparin-bound
FGF2. Interacts with SOX2 and SOX3 (By similarity). Interacts with
FLRT1, FLRT2 and FLRT3. Found in a ternary complex with FGF1 and
ITGAV:ITGB3 (By similarity). {ECO:0000250|UniProtKB:P11362,
ECO:0000250|UniProtKB:P16092, ECO:0000269|PubMed:15117958}.
-!- INTERACTION:
P19327:Htr1a; NbExp=6; IntAct=EBI-2480918, EBI-6570156;
P10686:Plcg1; NbExp=2; IntAct=EBI-2480918, EBI-520788;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15117958};
Single-pass type I membrane protein {ECO:0000269|PubMed:15117958}.
Nucleus {ECO:0000269|PubMed:15117958}. Cytoplasm, cytosol
{ECO:0000269|PubMed:15117958}. Cytoplasmic vesicle {ECO:0000250}.
Note=After ligand binding, both receptor and ligand are rapidly
internalized. Can translocate to the nucleus after
internalization, or by translocation from the endoplasmic
reticulum or Golgi apparatus to the cytosol, and from there to the
nucleus (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the parathyroid.
{ECO:0000269|PubMed:17992255}.
-!- DOMAIN: The second and third Ig-like domains directly interact
with fibroblast growth factors (FGF) and heparan sulfate
proteoglycans. Isoforms lacking the first Ig-like domain have
higher affinity for fibroblast growth factors (FGF) and heparan
sulfate proteoglycans than isoforms with all three Ig-like domains
(By similarity). {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 and proceeds in a highly ordered manner.
Initial autophosphorylation at Tyr-653 increases the kinase
activity by a factor of 50 to 100. After this, Tyr-583 becomes
phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766,
Tyr-583 and Tyr-585. In a third stage, Tyr-654 is
autophosphorylated, resulting in a further tenfold increase of
kinase activity. Phosphotyrosine residues provide docking sites
for interacting proteins and so are crucial for FGFR1 function and
its regulation (By similarity). {ECO:0000250|UniProtKB:P11362}.
-!- PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after
autophosphorylation, leading to internalization and lysosomal
degradation. CBL is recruited to activated FGFR1 via FRS2 and
GRB2, and mediates ubiquitination and subsequent degradation of
FGFR1 (By similarity). {ECO:0000250|UniProtKB:P11362}.
-!- 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|UniProtKB:P11362}.
-!- 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; D12498; BAA02059.1; -; mRNA.
PIR; S29840; S29840.
RefSeq; NP_077060.1; NM_024146.1.
UniGene; Rn.207203; -.
UniGene; Rn.9797; -.
ProteinModelPortal; Q04589; -.
SMR; Q04589; -.
BioGrid; 249399; 2.
CORUM; Q04589; -.
IntAct; Q04589; 4.
MINT; MINT-1520059; -.
STRING; 10116.ENSRNOP00000036885; -.
iPTMnet; Q04589; -.
PaxDb; Q04589; -.
PRIDE; Q04589; -.
GeneID; 79114; -.
KEGG; rno:79114; -.
UCSC; RGD:620713; rat.
CTD; 2260; -.
RGD; 620713; Fgfr1.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; Q04589; -.
KO; K04362; -.
PhylomeDB; Q04589; -.
BRENDA; 2.7.10.1; 5301.
PRO; PR:Q04589; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0090722; F:receptor-receptor interaction; ISO:RGD.
GO; GO:0001525; P:angiogenesis; ISO:RGD.
GO; GO:0060117; P:auditory receptor cell development; ISO:RGD.
GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
GO; GO:0007420; P:brain development; ISO:RGD.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISO:RGD.
GO; GO:0048469; P:cell maturation; ISO:RGD.
GO; GO:0071420; P:cellular response to histamine; IEP:RGD.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0021954; P:central nervous system neuron development; IMP:RGD.
GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; ISO:RGD.
GO; GO:0048699; P:generation of neurons; ISO:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
GO; GO:0030324; P:lung development; ISO:RGD.
GO; GO:0060484; P:lung-associated mesenchyme development; ISO:RGD.
GO; GO:0048762; P:mesenchymal cell differentiation; ISO:RGD.
GO; GO:0030901; P:midbrain development; ISO:RGD.
GO; GO:0042474; P:middle ear morphogenesis; ISO:RGD.
GO; GO:0021837; P:motogenic signaling involved in postnatal olfactory bulb interneuron migration; IMP:RGD.
GO; GO:0090272; P:negative regulation of fibroblast growth factor production; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0031175; P:neuron projection development; IDA:RGD.
GO; GO:0021769; P:orbitofrontal cortex development; ISO:RGD.
GO; GO:0001759; P:organ induction; ISO:RGD.
GO; GO:0042473; P:outer ear morphogenesis; ISO:RGD.
GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD.
GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; ISO:RGD.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; ISO:RGD.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:RGD.
GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; ISO:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; ISO:RGD.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; ISO:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IDA:RGD.
GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; ISO:RGD.
GO; GO:0051174; P:regulation of phosphorus metabolic process; ISO:RGD.
GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
GO; GO:0072091; P:regulation of stem cell proliferation; IMP:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0007435; P:salivary gland morphogenesis; ISO:RGD.
GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
GO; GO:0019827; P:stem cell population maintenance; IMP:RGD.
GO; GO:0001657; P:ureteric bud development; ISO:RGD.
GO; GO:0007037; P:vacuolar phosphate transport; ISO:RGD.
GO; GO:0021847; P:ventricular zone neuroblast division; ISO:RGD.
GO; GO:0070640; P:vitamin D3 metabolic process; ISO:RGD.
GO; GO:0042060; P:wound healing; IEP:RGD.
CDD; cd05098; PTKc_FGFR1; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR028174; FGF_rcpt_1.
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; IPR013151; Immunoglobulin.
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; 2.
Pfam; PF00047; ig; 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;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Heparin-binding;
Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 822 Fibroblast growth factor receptor 1.
/FTId=PRO_0000016782.
TOPO_DOM 22 376 Extracellular. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 822 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 119 Ig-like C2-type 1.
DOMAIN 158 246 Ig-like C2-type 2.
DOMAIN 255 357 Ig-like C2-type 3.
DOMAIN 478 767 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 484 490 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 562 564 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 160 177 Heparin-binding.
ACT_SITE 623 623 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 514 514 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 568 568 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 627 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 641 641 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 766 766 Mediates interaction with PLCG1 and SHB.
{ECO:0000250}.
MOD_RES 463 463 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 583 583 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 585 585 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 653 653 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 654 654 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 730 730 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 766 766 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 178 230 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 277 341 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 822 AA; 91825 MW; E59D924D0A1DE5C5 CRC64;
MWGWRGLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD
VQSINWLRDG VQLAESNRTR ITGEEVEVRD SIPADSGLYA CVTNSPSGSD TTYFSVNVSD
ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS
SGTPSPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN
HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
GPDNLPYDQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE
ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIIYKMK SGTKKSDFHS QMAVHKLAKS
IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL
GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK
HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL
VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG
RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP NPGVPVEELF KLLKEGHRMD
KPSNCTNELY MMMRDCWNAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQDSPSF
PDTRSSTCSS GEDSVFSHEP FPEEPCLPRH PTQLANGGLN RR


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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
10-271-82072 Fibroblast Growth Factor-basic Human - HBGF-2; Basic fibroblast growth factor; BFGF; Prostatropin 0.05 mg
10-271-82072 Fibroblast Growth Factor-basic Human - HBGF-2; Basic fibroblast growth factor; BFGF; Prostatropin 0.01 mg
300-003 FGF-2 (basic) Human Host: E. coli FGF2; BFGF; FGFB; HBGF-2; basic Fibroblast growth factor (bFGF); Heparin binding growth factor-2 50
300-002 FGF-2 (basic) Human Host: E. coli FGF2; BFGF; FGFB; HBGF-2; basic Fibroblast growth factor (bFGF); Heparin binding growth factor-2 25
300-001 FGF-2 (basic) Human Host: E. coli FGF2; BFGF; FGFB; HBGF-2; basic Fibroblast growth factor (bFGF); Heparin binding growth factor-2 10
10-664-50009 Fibroblast growth factor receptor 3 - EC 2.7.10.1; FGFR-3; CD333 antigen N_A 0.1 mg
U0551b CLIA Basic fibroblast growth factor,bFGF,Bos taurus,Bovine,FGF2,FGF-2,HBGF-2,Heparin-binding growth factor 2 96T
E0551m ELISA kit Basic fibroblast growth factor,bFGF,Fgf2,Fgf-2,HBGF-2,Heparin-binding growth factor 2,Mouse,Mus musculus 96T
U0551m CLIA Basic fibroblast growth factor,bFGF,Fgf2,Fgf-2,HBGF-2,Heparin-binding growth factor 2,Mouse,Mus musculus 96T
E0551b ELISA kit Basic fibroblast growth factor,bFGF,Bos taurus,Bovine,FGF2,FGF-2,HBGF-2,Heparin-binding growth factor 2 96T
E0551r ELISA Basic fibroblast growth factor,bFGF,Fgf2,Fgf-2,HBGF-2,Heparin-binding growth factor 2,Rat,Rattus norvegicus 96T
E0551r ELISA kit Basic fibroblast growth factor,bFGF,Fgf2,Fgf-2,HBGF-2,Heparin-binding growth factor 2,Rat,Rattus norvegicus 96T
E0551b ELISA Basic fibroblast growth factor,bFGF,Bos taurus,Bovine,FGF2,FGF-2,HBGF-2,Heparin-binding growth factor 2 96T


 

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