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Fibroblast growth factor 13 (FGF-13) (Fibroblast growth factor homologous factor 2) (FHF-2)

 FGF13_MOUSE             Reviewed;         245 AA.
P70377; B1AU21; O35338; Q3UR31; Q8VCY9; Q9JLA5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 124.
RecName: Full=Fibroblast growth factor 13;
Short=FGF-13;
AltName: Full=Fibroblast growth factor homologous factor 2;
Short=FHF-2;
Name=Fgf13; Synonyms=Fhf2;
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).
TISSUE=Eye;
PubMed=8790420; DOI=10.1073/pnas.93.18.9850;
Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H.,
Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.;
"Fibroblast growth factor (FGF) homologous factors: new members of the
FGF family implicated in nervous system development.";
Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=9232594; DOI=10.1016/S0925-4773(97)00042-7;
Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D.,
Goldfarb M.;
"Murine FGF-12 and FGF-13: expression in embryonic nervous system,
connective tissue and heart.";
Mech. Dev. 64:31-39(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 3), ALTERNATIVE SPLICING,
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=10644718; DOI=10.1074/jbc.275.4.2589;
Munoz-Sanjuan I., Smallwood P.M., Nathans J.;
"Isoform diversity among fibroblast growth factor homologous factors
is generated by alternative promoter usage and differential
splicing.";
J. Biol. Chem. 275:2589-2597(2000).
[8]
FUNCTION IN MAPK SIGNALING, AND INTERACTION WITH MAPK8IP2.
PubMed=11378392; DOI=10.1016/S0960-9822(01)00232-9;
Schoorlemmer J., Goldfarb M.;
"Fibroblast growth factor homologous factors are intracellular
signaling proteins.";
Curr. Biol. 11:793-797(2001).
[9]
FUNCTION IN MAPK SIGNALING.
PubMed=12244047; DOI=10.1074/jbc.M205520200;
Schoorlemmer J., Goldfarb M.;
"Fibroblast growth factor homologous factors and the islet brain-2
scaffold protein regulate activation of a stress-activated protein
kinase.";
J. Biol. Chem. 277:49111-49119(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart;
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).
[11]
FUNCTION IN SODIUM CHANNEL REGULATION, TISSUE SPECIFICITY, INTERACTION
WITH SCN5A, AND SUBCELLULAR LOCATION.
PubMed=21817159; DOI=10.1161/CIRCRESAHA.111.247957;
Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V.,
Puranam R.S., Rosenberg P.B., Bursac N., Pitt G.S.;
"Fibroblast growth factor homologous factor 13 regulates Na+ channels
and conduction velocity in murine hearts.";
Circ. Res. 109:775-782(2011).
[12]
FUNCTION IN NEURON POLARIZATION, FUNCTION IN NEURON MIGRATION,
DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TUBULIN-BINDING.
PubMed=22726441; DOI=10.1016/j.cell.2012.04.046;
Wu Q.F., Yang L., Li S., Wang Q., Yuan X.B., Gao X., Bao L., Zhang X.;
"Fibroblast growth factor 13 is a microtubule-stabilizing protein
regulating neuronal polarization and migration.";
Cell 149:1549-1564(2012).
-!- FUNCTION: Microtubule-binding protein which directly binds tubulin
and is involved in both polymerization and stabilization of
microtubules. Through its action on microtubules, may participate
to the refinement of axons by negatively regulating axonal and
leading processes branching. Plays a crucial role in neuron
polarization and migration in the cerebral cortex and the
hippocampus.
-!- FUNCTION: Isoform 1 seems not to be involved in neuroblast
polarization and migration but regulates axon branching.
-!- FUNCTION: May regulate voltage-gated sodium channels transport and
function.
-!- FUNCTION: May also play a role in MAPK signaling.
-!- SUBUNIT: Interacts with SCN8A; may regulate SCN8A activity (By
similarity). Interacts with SCN1A; may regulate SCN1A activity (By
similarity). Interacts with SCN5A; the interaction is direct and
may regulate SNC5A density at membranes and function. Interacts
with MAPK8IP2; may regulate the MAPK8IP2 scaffolding activity.
{ECO:0000250, ECO:0000269|PubMed:11378392,
ECO:0000269|PubMed:21817159}.
-!- SUBCELLULAR LOCATION: Cell projection, filopodium. Cell
projection, growth cone. Cell projection, dendrite. Nucleus.
Cytoplasm. Note=Not secreted. Localizes to the lateral membrane
and intercalated disks of myocytes.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=FGF13A, mFHF-2(1S), FGF13-S;
IsoId=P70377-1; Sequence=Displayed;
Name=2; Synonyms=FGF13B, mFHF-2(1U), FGF13-U;
IsoId=P70377-2; Sequence=VSP_044131;
Name=3; Synonyms=FGF13-VY, mFHF-2(1Y+1V);
IsoId=P70377-3; Sequence=VSP_044130;
-!- TISSUE SPECIFICITY: Detected in brain, eye and heart. In brain,
the different isoforms display different patterns of expression.
Expressed in brain and heart (at protein level). Isoform 3 is
highly expressed in cardiac myocytes while isoform 1 is the most
abundant in brain. {ECO:0000269|PubMed:10644718,
ECO:0000269|PubMed:21817159, ECO:0000269|PubMed:9232594}.
-!- DEVELOPMENTAL STAGE: Expressed in the subplate of the embryonic
cortex and the axonal tracts in the intermediate zone, and in
axonal tracts of projection neurons, specifically in the
corticothalamic tract and the corpus callosum (at protein level).
Isoform 2 is transiently expressed in the neocortex and
hippocampus from E17 to P7 (at protein level). In embryonic brain,
present in all divisions of the central and peripheral nervous
system and it is at least 5 times more abundant than other FHFs.
Detected in the subplate, ganglionic eminences, and proliferative
zones of the cortical wall at E14. Detected in the cortical plate
of the cerebral cortex, hippocampus, and striatum from E17 to P14.
Expression is markedly reduced in adult brain where it is most
abundant in hippocampus. Also detected in developing kidney.
{ECO:0000269|PubMed:9232594}.
-!- PTM: May be phosphorylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Conditional knockout mice lacking fgf13 in
the cerebral cortex or mice lacking fgf13 in most tissues display
similar phenotypes of impaired spatial acquisition and memory. The
cued memory and the capacity of novel object recognition are
altered. They also display anxiety-related and reduced depression-
like behaviors. This is associated with a disorganization of
cortical structure and neural circuits. The laminar formation of
the neocortex is delayed and the hippocampal development is also
affected. {ECO:0000269|PubMed:22726441}.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U66202; AAB18918.1; -; mRNA.
EMBL; AF020737; AAB71606.1; -; mRNA.
EMBL; AK141848; BAE24857.1; -; mRNA.
EMBL; AL669891; CAM19176.1; -; Genomic_DNA.
EMBL; AL672247; CAM19176.1; JOINED; Genomic_DNA.
EMBL; AL713968; CAM19176.1; JOINED; Genomic_DNA.
EMBL; AL713968; CAM22824.1; -; Genomic_DNA.
EMBL; AL672247; CAM22824.1; JOINED; Genomic_DNA.
EMBL; AL713968; CAM22825.1; -; Genomic_DNA.
EMBL; AL672247; CAM22825.1; JOINED; Genomic_DNA.
EMBL; AL713968; CAM22827.1; -; Genomic_DNA.
EMBL; AL669891; CAM22827.1; JOINED; Genomic_DNA.
EMBL; AL672247; CAM22827.1; JOINED; Genomic_DNA.
EMBL; AL672247; CAM27417.1; -; Genomic_DNA.
EMBL; AL713968; CAM27417.1; JOINED; Genomic_DNA.
EMBL; AL672247; CAM27418.1; -; Genomic_DNA.
EMBL; AL713968; CAM27418.1; JOINED; Genomic_DNA.
EMBL; AL672247; CAM27420.1; -; Genomic_DNA.
EMBL; AL669891; CAM27420.1; JOINED; Genomic_DNA.
EMBL; AL713968; CAM27420.1; JOINED; Genomic_DNA.
EMBL; CH466583; EDL42180.1; -; Genomic_DNA.
EMBL; CH466583; EDL42182.1; -; Genomic_DNA.
EMBL; BC018238; AAH18238.1; -; mRNA.
EMBL; AF199608; AAF31395.1; -; mRNA.
CCDS; CCDS30157.1; -. [P70377-1]
CCDS; CCDS72383.1; -. [P70377-2]
RefSeq; NP_001277344.1; NM_001290415.1. [P70377-2]
RefSeq; NP_034330.2; NM_010200.3. [P70377-1]
UniGene; Mm.7995; -.
ProteinModelPortal; P70377; -.
SMR; P70377; -.
STRING; 10090.ENSMUSP00000033473; -.
iPTMnet; P70377; -.
PhosphoSitePlus; P70377; -.
PaxDb; P70377; -.
PeptideAtlas; P70377; -.
PRIDE; P70377; -.
TopDownProteomics; P70377-2; -. [P70377-2]
Ensembl; ENSMUST00000033473; ENSMUSP00000033473; ENSMUSG00000031137. [P70377-1]
Ensembl; ENSMUST00000119306; ENSMUSP00000113206; ENSMUSG00000031137. [P70377-2]
GeneID; 14168; -.
KEGG; mmu:14168; -.
UCSC; uc009tht.3; mouse. [P70377-1]
UCSC; uc009thu.3; mouse. [P70377-2]
UCSC; uc009thv.2; mouse. [P70377-3]
CTD; 2258; -.
MGI; MGI:109178; Fgf13.
eggNOG; KOG3885; Eukaryota.
eggNOG; ENOG4111IPH; LUCA.
GeneTree; ENSGT00760000118859; -.
HOGENOM; HOG000290676; -.
HOVERGEN; HBG007580; -.
InParanoid; P70377; -.
KO; K04358; -.
OMA; KSNACRC; -.
OrthoDB; EOG091G0NAY; -.
TreeFam; TF317805; -.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
ChiTaRS; Fgf13; mouse.
PRO; PR:P70377; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031137; -.
CleanEx; MM_FGF13; -.
ExpressionAtlas; P70377; baseline and differential.
Genevisible; P70377; MM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:InterPro.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0008083; F:growth factor activity; IEA:InterPro.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
GO; GO:0017080; F:sodium channel regulator activity; IMP:UniProtKB.
GO; GO:0021795; P:cerebral cortex cell migration; IMP:UniProtKB.
GO; GO:0045200; P:establishment of neuroblast polarity; IMP:UniProtKB.
GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
GO; GO:0007612; P:learning; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; ISO:MGI.
GO; GO:0007613; P:memory; IMP:UniProtKB.
GO; GO:0046785; P:microtubule polymerization; IMP:UniProtKB.
GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL.
GO; GO:1990834; P:response to odorant; IEA:Ensembl.
GO; GO:0006814; P:sodium ion transport; IMP:BHF-UCL.
CDD; cd00058; FGF; 1.
InterPro; IPR028279; FGF13.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF77; PTHR11486:SF77; 1.
Pfam; PF00167; FGF; 1.
PRINTS; PR00263; HBGFFGF.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00247; HBGF_FGF; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Complete proteome; Cytoplasm;
Microtubule; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 245 Fibroblast growth factor 13.
/FTId=PRO_0000147608.
REGION 1 62 Mediates targeting to the nucleus.
REGION 67 201 Mediates interaction with sodium
channels. {ECO:0000250}.
REGION 157 164 Tubulin-binding domain necessary and
sufficient for tubulin-binding.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 63 MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKN
KLNVFSRVKLFGSKKRRRRRPE -> MSGKVTKPKEEKDAS
KVLDDAPPGTQEYIMLRQDSIQSAELKKKESPFRAKCHEIF
CCPPKQVHHKENTEPEE (in isoform 3).
{ECO:0000303|PubMed:10644718}.
/FTId=VSP_044130.
VAR_SEQ 1 62 MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKN
KLNVFSRVKLFGSKKRRRRRP -> MALLRKSYS (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_044131.
CONFLICT 2 2 A -> T (in Ref. 1; AAB18918).
{ECO:0000305}.
CONFLICT 2 2 Missing (in Ref. 2; AAB71606).
{ECO:0000305}.
CONFLICT 199 199 L -> Q (in Ref. 2; AAB71606).
{ECO:0000305}.
SEQUENCE 245 AA; 27588 MW; 5B96D41AC3A3DF78 CRC64;
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR
RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK
LYLAMNSEGY LYTSEHFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM
KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS
HNEST


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U0636m CLIA 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 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
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
U0636r CLIA 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
E0636p ELISA FGF7,FGF-7,Fibroblast growth factor 7,HBGF-7,Heparin-binding growth factor 7,Keratinocyte growth factor,KGF,Pig,Sus scrofa 96T


 

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