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Myoblast growth factor receptor egl-15 (EC 2.7.10.1) (Egg-laying defective protein 15)

 EGL15_CAEEL             Reviewed;        1040 AA.
Q10656; Q7JL68; Q7YZM7; Q7YZM8; Q7YZN0; Q7YZN1; Q7Z025; Q8MQ14;
Q93804; Q95QE0; Q95QE1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
05-JUL-2017, entry version 160.
RecName: Full=Myoblast growth factor receptor egl-15;
EC=2.7.10.1;
AltName: Full=Egg-laying defective protein 15;
Flags: Precursor;
Name=egl-15; ORFNames=F58A3.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF GLU-680 AND PRO-714.
STRAIN=Bristol N2;
PubMed=7585964; DOI=10.1016/0092-8674(95)90101-9;
Devore D.L., Horvitz H.R., Stern M.J.;
"An FGF receptor signaling pathway is required for the normal cell
migrations of the sex myoblasts in C. elegans hermaphrodites.";
Cell 83:611-620(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF
932-1040 (ISOFORMS A; C; D AND E), AND FUNCTION.
PubMed=12835392; DOI=10.1242/dev.00604;
Goodman S.J., Branda C.S., Robinson M.K., Burdine R.D., Stern M.J.;
"Alternative splicing affecting a novel domain in the C. elegans EGL-
15 FGF receptor confers functional specificity.";
Development 130:3757-3766(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
DEPHOSPHORYLATION BY CLR-1.
STRAIN=Bristol N2;
PubMed=9585503; DOI=10.1101/gad.12.10.1425;
Kokel M., Borland C.Z., DeLong L., Horvitz H.R., Stern M.J.;
"clr-1 encodes a receptor tyrosine phosphatase that negatively
regulates an FGF receptor signaling pathway in Caenorhabditis
elegans.";
Genes Dev. 12:1425-1437(1998).
[5]
FUNCTION.
PubMed=11689700; DOI=10.1128/MCB.21.23.8104-8116.2001;
Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
Stern M.J.;
"The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-
like multisubstrate adaptor protein in fibroblast growth factor signal
transduction.";
Mol. Cell. Biol. 21:8104-8116(2001).
[6]
FUNCTION.
PubMed=14517244; DOI=10.1093/emboj/cdg472;
Szewczyk N.J., Jacobson L.A.;
"Activated EGL-15 FGF receptor promotes protein degradation in muscles
of Caenorhabditis elegans.";
EMBO J. 22:5058-5067(2003).
[7]
FUNCTION.
PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D.,
Yates J.R. III, Schafer W.R.;
"Identification and characterization of novel nicotinic receptor-
associated proteins in Caenorhabditis elegans.";
EMBO J. 24:2566-2578(2005).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-714.
PubMed=16495308; DOI=10.1242/dev.02300;
Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
"FGF negatively regulates muscle membrane extension in Caenorhabditis
elegans.";
Development 133:1263-1275(2006).
-!- FUNCTION: Receptor tyrosine kinase required for larval development
(PubMed:7585964). May phosphorylate adapter protein soc-1 which in
turn may result in the recruitment and/or activation of
phosphatase ptp-2 (PubMed:11689700). May activate the Ras/MAPK
kinase signaling pathway which includes sem-5, sos-1, let-60/Ras,
lin-45/Raf, mek-2 and mpk-1 (PubMed:11689700). Acts in the
hypodermis to regulate axon growth and fluid homeostasis
(PubMed:12835392, PubMed:7585964). Activates protein degradation
in muscles (PubMed:14517244). Probably following interaction with
ligand let-756, regulates negatively membrane protrusion from body
wall muscles during larval development (PubMed:16495308). Plays a
role in nicotinic acetylcholine receptor (nAChR)-mediated
sensitivity to nicotine (PubMed:15990870). Regulates synaptic
levels of nAChR subunit lev-1 in the nerve cord (PubMed:15990870).
{ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:12835392,
ECO:0000269|PubMed:14517244, ECO:0000269|PubMed:15990870,
ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:7585964}.
-!- FUNCTION: Isoform b: Affects the maintenance of axon position
without affecting axon growth. Interaction with egl-17 is required
for the guidance of sex myoblast migration during gonad
development. {ECO:0000269|PubMed:12835392}.
-!- FUNCTION: Isoform a: Interaction with let-756 appears to play a
role in maintaining body morphology at higher temperatures.
{ECO:0000269|PubMed:12835392}.
-!- FUNCTION: Isoform c: Interaction with let-756 appears to play a
role in maintaining body morphology at higher temperatures.
{ECO:0000269|PubMed:12835392}.
-!- FUNCTION: Isoform d: Interaction with let-756 appears to play a
role in maintaining body morphology at higher temperatures.
{ECO:0000269|PubMed:12835392}.
-!- FUNCTION: Isoform e: Interaction with let-756 appears to play a
role in maintaining body morphology at higher temperatures.
{ECO:0000269|PubMed:12835392}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=a;
IsoId=Q10656-1; Sequence=Displayed;
Name=b; Synonyms=EGL-15(5A);
IsoId=Q10656-2; Sequence=VSP_019861;
Name=c;
IsoId=Q10656-3; Sequence=VSP_002991, VSP_002992, VSP_002994;
Name=d;
IsoId=Q10656-4; Sequence=VSP_002991, VSP_002992, VSP_019862;
Name=e;
IsoId=Q10656-5; Sequence=VSP_002991, VSP_002992, VSP_019863;
-!- PTM: Activity is regulated by the phosphatase clr-1, however it is
not known whether clr-1 acts directly on egl-15.
{ECO:0000269|PubMed:9585503}.
-!- DISRUPTION PHENOTYPE: Early arrest in larval development. Impaired
guided migration of sex myoblasts (PubMed:7585964). RNAi-mediated
knockdown causes ectopic membrane extension from body wall muscles
(PubMed:16495308). {ECO:0000269|PubMed:16495308,
ECO:0000269|PubMed:7585964}.
-!- 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; U39761; AAC46934.1; -; mRNA.
EMBL; AY268435; AAP31029.1; -; mRNA.
EMBL; AY268436; AAP31030.1; -; mRNA.
EMBL; AY288941; AAP44084.1; -; mRNA.
EMBL; AY288942; AAP44085.1; -; mRNA.
EMBL; AY292532; AAP74805.1; -; mRNA.
EMBL; Z81017; CAB02673.2; -; Genomic_DNA.
EMBL; Z81017; CAC70094.2; -; Genomic_DNA.
EMBL; Z81017; CAC70095.2; -; Genomic_DNA.
EMBL; Z81017; CAD44136.1; -; Genomic_DNA.
EMBL; Z81017; CAE47468.1; -; Genomic_DNA.
PIR; A57638; A57638.
PIR; T22889; T22889.
RefSeq; NP_001024723.1; NM_001029552.2. [Q10656-2]
RefSeq; NP_001024724.3; NM_001029553.5.
RefSeq; NP_001024725.2; NM_001029554.4.
RefSeq; NP_001024726.2; NM_001029555.4.
RefSeq; NP_509842.2; NM_077441.6. [Q10656-1]
UniGene; Cel.17140; -.
ProteinModelPortal; Q10656; -.
SMR; Q10656; -.
BioGrid; 46202; 148.
IntAct; Q10656; 1.
STRING; 6239.F58A3.2c; -.
iPTMnet; Q10656; -.
PaxDb; Q10656; -.
PeptideAtlas; Q10656; -.
EnsemblMetazoa; F58A3.2a.1; F58A3.2a.1; WBGene00001184. [Q10656-1]
EnsemblMetazoa; F58A3.2a.2; F58A3.2a.2; WBGene00001184. [Q10656-1]
EnsemblMetazoa; F58A3.2a.3; F58A3.2a.3; WBGene00001184. [Q10656-1]
EnsemblMetazoa; F58A3.2a.4; F58A3.2a.4; WBGene00001184. [Q10656-1]
GeneID; 181291; -.
KEGG; cel:CELE_F58A3.2; -.
UCSC; F58A3.2e; c. elegans. [Q10656-1]
CTD; 181291; -.
WormBase; F58A3.2a; CE28238; WBGene00001184; egl-15. [Q10656-1]
WormBase; F58A3.2b; CE35726; WBGene00001184; egl-15. [Q10656-2]
WormBase; F58A3.2c; CE50149; WBGene00001184; egl-15.
WormBase; F58A3.2d; CE50303; WBGene00001184; egl-15.
WormBase; F58A3.2e; CE50247; WBGene00001184; egl-15.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
InParanoid; Q10656; -.
OrthoDB; EOG091G0CQZ; -.
PhylomeDB; Q10656; -.
BRENDA; 2.7.10.1; 1045.
Reactome; R-CEL-190322; FGFR4 ligand binding and activation.
Reactome; R-CEL-190370; FGFR1b ligand binding and activation.
Reactome; R-CEL-190371; FGFR3b ligand binding and activation.
Reactome; R-CEL-190372; FGFR3c ligand binding and activation.
Reactome; R-CEL-190373; FGFR1c ligand binding and activation.
Reactome; R-CEL-190375; FGFR2c ligand binding and activation.
Reactome; R-CEL-190377; FGFR2b ligand binding and activation.
Reactome; R-CEL-445144; Signal transduction by L1.
Reactome; R-CEL-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-CEL-5654221; Phospholipase C-mediated cascade, FGFR2.
Reactome; R-CEL-5654227; Phospholipase C-mediated cascade, FGFR3.
Reactome; R-CEL-5654228; Phospholipase C-mediated cascade, FGFR4.
Reactome; R-CEL-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-CEL-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-CEL-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-CEL-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-CEL-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-CEL-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-CEL-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-CEL-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-CEL-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-CEL-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-CEL-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-CEL-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
SignaLink; Q10656; -.
PRO; PR:Q10656; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00001184; -.
ExpressionAtlas; Q10656; baseline.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0016477; P:cell migration; IMP:WormBase.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:WormBase.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:WormBase.
GO; GO:0007517; P:muscle organ development; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0018991; P:oviposition; IMP:WormBase.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
GO; GO:0031344; P:regulation of cell projection organization; IMP:WormBase.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom.
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; 3.
Pfam; PF07714; Pkinase_Tyr; 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; ATP-binding; Complete proteome;
Developmental protein; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1040 Myoblast growth factor receptor egl-15.
/FTId=PRO_0000016796.
TOPO_DOM 20 525 Extracellular. {ECO:0000255}.
TRANSMEM 526 549 Helical. {ECO:0000255}.
TOPO_DOM 550 1040 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 125 Ig-like C2-type 1.
DOMAIN 287 383 Ig-like C2-type 2.
DOMAIN 391 501 Ig-like C2-type 3.
DOMAIN 640 931 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 646 654 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 797 797 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 672 672 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 828 828 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 474 474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 497 497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 314 367 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 414 485 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 129 245 FCDYFLFPDIHHLNIPMECVCLWKYNKEAKRSDVNYAAVTG
EVCSKYASRMINRARKPLPMIPCFGDHCKEFDTTPVSDFGL
PGKPEDDPLVKRVVLKKDDVIVPVHDSEESPSESR -> PL
KLFDWLTEHRVFDISHLLPKLLPPAEMRRVKSQLGGWEKMN
NEQKIVRARHILRLRQINHALG (in isoform b).
{ECO:0000303|PubMed:12835392}.
/FTId=VSP_019861.
VAR_SEQ 829 829 R -> RL (in isoform c, isoform d and
isoform e).
{ECO:0000303|PubMed:12835392}.
/FTId=VSP_002991.
VAR_SEQ 984 984 E -> EVDQN (in isoform c, isoform d and
isoform e).
{ECO:0000303|PubMed:12835392}.
/FTId=VSP_002992.
VAR_SEQ 1027 1040 RIPSNNNSMSKPEF -> LYIHKVLNEPIGNGYVRQDKLAR
AVSGVANQSLDSALGSPAWPSYDRPSNKASCLDQTHQYYNT
TSKIQYLHFTFDDPDCMTRSRDSAIFEESYHPNYIQSHPLY
SKIIIKKNMTPRNPLPTKETIV (in isoform c).
{ECO:0000303|PubMed:12835392}.
/FTId=VSP_002994.
VAR_SEQ 1027 1040 RIPSNNNSMSKPEF -> LYIHKVLNEPIGNGYVRQDKLAR
AVSGVANQSLDSALGSPAWPSYDRPSNKASCLDDEKHHYYY
S (in isoform d).
{ECO:0000303|PubMed:12835392}.
/FTId=VSP_019862.
VAR_SEQ 1027 1040 RIPSNNNSMSKPEF -> LYIHKVLNEPIGNGSNSPVL
(in isoform e).
{ECO:0000303|PubMed:12835392}.
/FTId=VSP_019863.
MUTAGEN 680 680 E->K: In n1775; loss of activity.
{ECO:0000269|PubMed:7585964}.
MUTAGEN 714 714 P->L: In n1783; loss of activity. Ectopic
membrane extension in body wall muscles.
{ECO:0000269|PubMed:16495308,
ECO:0000269|PubMed:7585964}.
CONFLICT 551 551 Q -> G (in Ref. 2; AAP44084).
{ECO:0000305}.
SEQUENCE 1040 AA; 118956 MW; 8CA227195DDBCD69 CRC64;
MSYFLASCLG VGLLSTVSCS LQGLTSHYRE NIPRFKHVAN ERYEVFLGDE IKFDCQTAAS
KISAFVEWYR NDKLLKNDQI DKDKIRKDNN RMMLHLKNID VSDQGLWSCR VHNAYGQISR
NFTVEVIDFC DYFLFPDIHH LNIPMECVCL WKYNKEAKRS DVNYAAVTGE VCSKYASRMI
NRARKPLPMI PCFGDHCKEF DTTPVSDFGL PGKPEDDPLV KRVVLKKDDV IVPVHDSEES
PSESRTEFIN ADEKENKEDE EEDYSVSQPV APDAGLTELN ITAEEPPYFK SNDNIVLFNE
THALPAGRTL KLNCRAKGYP EPQIIWYKNG KMLKKSSARS GGYEFKFNRW SLEVEDAVVA
DSGEFHCEAL NKVGSAKKYF HVIIVNRMRR PPIIVPNILA NQSVNINDTA TFHCKVVSDL
LPHIIWVRIN KINGSYSYYN NSAEEYMFNY TEMDTFDKAH VHHVGDESTL TIFNVSLDDQ
GIYACLSGNS LGMSMANATL TVNEFMAIHL LTGDEPKIDR WTTSDYIFTT ILLFLLLAAT
LFGILFMVCK QTLHKKGFMD DTVGLVARKK RVVVSKRPMN EDNENSDDEP SPYQIQIIET
PITKKEAARK QRKRMNSENT VLSEYEVDSD PVWEVERSKL SLVHMLGEGA FGEVWKATYK
ETENNEIAVA VKKLKMSAHE KELIDLVSEM ETFKVIGEHE NVLRLIGCCT GAGPLYVVVE
LCKHGNLRDF LRAHRPKEEK AKKSSQELTD YLEPRKASDK DDIELIPNLT QRHLVQFAWQ
VAQGMNFLAS KKIIHRDLAA RNVLVGDGHV LKISDFGLSR DVHCNDYYRK RGNGRLPIKW
MALEALDSNV YTVESDVWSY GVLLWEIMTL GGTPYPTIAM PELYANLKEG YRMEPPHLCP
QEVYHLMCSC WREKLEERPS FKTIVDYLDW MLTMTNETIE GSQEFNDQFF SERSTASGPV
SPMESFQKKR KHRPLSAPVN LPSEPQHTIC DDYESNFSVE PPNDPNHLYC NDNMLKNHII
TPETSQRIPS NNNSMSKPEF


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U0074r CLIA Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Proto-oncogene c-Fgr,Rat,Rattus norvegicus 96T
E0074m ELISA kit Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Mouse,Mus musculus,Proto-oncogene c-Fgr 96T
E0074r ELISA Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Proto-oncogene c-Fgr,Rat,Rattus norvegicus 96T
E0074m ELISA Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Mouse,Mus musculus,Proto-oncogene c-Fgr 96T
E0074r ELISA kit Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Proto-oncogene c-Fgr,Rat,Rattus norvegicus 96T
103-M35 VEGFR-2_FLK-1 Anti-Mouse Host: Rat vascular endothelial growth factor receptor-2 ; Kdr; Ly73; Flk-1; VEGF receptor 2; kinase insert domain protein receptor 100
103-M32 VEGFR-2_Flk-1 Anti-Mouse Host: Rat vascular endothelial growth factor receptor-2 ; Kdr; Ly73; Flk-1; VEGF receptor 2; kinase insert domain protein receptor 100


 

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