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Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)

 PDGFA_HUMAN             Reviewed;         211 AA.
P04085; B5BU73;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1986, sequence version 1.
12-SEP-2018, entry version 188.
RecName: Full=Platelet-derived growth factor subunit A;
Short=PDGF subunit A;
AltName: Full=PDGF-1;
AltName: Full=Platelet-derived growth factor A chain;
AltName: Full=Platelet-derived growth factor alpha polypeptide;
Flags: Precursor;
Name=PDGFA; Synonyms=PDGF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3422746; DOI=10.1073/pnas.85.5.1492;
Bonthron D.T., Morton C.C., Orkin S.H., Collins T.;
"Platelet-derived growth factor A chain: gene structure, chromosomal
location, and basis for alternative mRNA splicing.";
Proc. Natl. Acad. Sci. U.S.A. 85:1492-1496(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2832727; DOI=10.1128/MCB.8.2.571;
Rorsman F., Bywater M., Knott T.J., Scott J., Betsholtz C.;
"Structural characterization of the human platelet-derived growth
factor A-chain cDNA and gene: alternative exon usage predicts two
different precursor proteins.";
Mol. Cell. Biol. 8:571-577(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3754619; DOI=10.1038/320695a0;
Betsholtz C., Johnsson A., Heldin C.H., Westermark B., Lind P.,
Urdea M.S., Eddy R., Shows T.B., Philpott K., Mellor A.L., Knott T.J.,
Scott J.;
"cDNA sequence and chromosomal localization of human platelet-derived
growth factor A-chain and its expression in tumour cell lines.";
Nature 320:695-699(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3666150; DOI=10.1016/0014-5793(87)80297-1;
Hoppe J., Schumacher L., Eichner W., Weich H.A.;
"The long 3'-untranslated regions of the PDGF-A and -B mRNAs are only
distantly related.";
FEBS Lett. 223:243-246(1987).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
PubMed=8486521;
Takimoto Y., Li W.Y., Wang Z.Y., Tong B.D., Deuel T.F.;
"Nucleotide sequence of the 5' region of the human platelet-derived
growth factor A-chain gene.";
Hiroshima J. Med. Sci. 42:47-52(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-211.
PubMed=1612586; DOI=10.1016/0888-7543(92)90240-S;
Bonthron D., Collins T., Grzeschik K.H., van Roy N., Speleman F.;
"Platelet-derived growth factor A chain: confirmation of localization
of PDGFA to chromosome 7p22 and description of an unusual
minisatellite.";
Genomics 13:257-263(1992).
[9]
ALTERNATIVE SPLICING.
PubMed=3614363; DOI=10.1038/328619a0;
Tong B.D., Auer D.E., Jaye M., Kaplow J.M., Ricca G., McConathy E.,
Drohan W., Deuel T.F.;
"cDNA clones reveal differences between human glial and endothelial
cell platelet-derived growth factor A-chains.";
Nature 328:619-621(1987).
[10]
ALTERNATIVE SPLICING.
PubMed=3614364; DOI=10.1038/328621a0;
Collins T., Bonthron D.T., Orkin S.H.;
"Alternative RNA splicing affects function of encoded platelet-derived
growth factor A chain.";
Nature 328:621-624(1987).
[11]
INTERCHAIN DISULFIDE BONDS.
PubMed=1317862;
Andersson M., Oestman A., Baeckstroem G., Hellman U.,
George-Nascimento C., Westermark B., Heldin C.-H.;
"Assignment of interchain disulfide bonds in platelet-derived growth
factor (PDGF) and evidence for agonist activity of monomeric PDGF.";
J. Biol. Chem. 267:11260-11266(1992).
[12]
INTERACTION WITH CSPG4.
PubMed=10358027; DOI=10.1074/jbc.274.24.16831;
Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.;
"High-affinity binding of basic fibroblast growth factor and platelet-
derived growth factor-AA to the core protein of the NG2
proteoglycan.";
J. Biol. Chem. 274:16831-16837(1999).
[13]
REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE.
PubMed=18483217; DOI=10.1101/gad.1653708;
Andrae J., Gallini R., Betsholtz C.;
"Role of platelet-derived growth factors in physiology and medicine.";
Genes Dev. 22:1276-1312(2008).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-181, AND DISULFIDE BONDS.
PubMed=20534510; DOI=10.1073/pnas.1000806107;
Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
"Structures of a platelet-derived growth factor/propeptide complex and
a platelet-derived growth factor/receptor complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
-!- FUNCTION: Growth factor that plays an essential role in the
regulation of embryonic development, cell proliferation, cell
migration, survival and chemotaxis. Potent mitogen for cells of
mesenchymal origin. Required for normal lung alveolar septum
formation during embryogenesis, normal development of the
gastrointestinal tract, normal development of Leydig cells and
spermatogenesis. Required for normal oligodendrocyte development
and normal myelination in the spinal cord and cerebellum. Plays an
important role in wound healing. Signaling is modulated by the
formation of heterodimers with PDGFB (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer; antiparallel disulfide-linked dimer.
Heterodimer with PDGFB; antiparallel disulfide-linked dimer. The
PDGFA homodimer interacts with PDGFRA homodimers, and with
heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed
of PDGFA and PDGFB interacts with PDGFRA homodimers, and with
heterodimers formed by PDGFRA and PDGFRB. Interacts with CSPG4.
{ECO:0000269|PubMed:10358027, ECO:0000269|PubMed:20534510}.
-!- INTERACTION:
P16234:PDGFRA; NbExp=6; IntAct=EBI-2881386, EBI-2861522;
-!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
wounding.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P04085-1; Sequence=Displayed;
Name=Short;
IsoId=P04085-2; Sequence=VSP_004602, VSP_004603;
-!- DOMAIN: The long form contains a basic insert which acts as a cell
retention signal.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
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EMBL; X03795; CAA27421.1; -; mRNA.
EMBL; X06374; CAA29677.1; -; mRNA.
EMBL; M20494; AAA60045.1; -; Genomic_DNA.
EMBL; M20488; AAA60045.1; JOINED; Genomic_DNA.
EMBL; M20489; AAA60045.1; JOINED; Genomic_DNA.
EMBL; M20490; AAA60045.1; JOINED; Genomic_DNA.
EMBL; M20491; AAA60045.1; JOINED; Genomic_DNA.
EMBL; M20492; AAA60045.1; JOINED; Genomic_DNA.
EMBL; M20493; AAA60045.1; JOINED; Genomic_DNA.
EMBL; M19988; AAA60046.1; -; Genomic_DNA.
EMBL; M21571; AAA60046.1; JOINED; Genomic_DNA.
EMBL; M19984; AAA60046.1; JOINED; Genomic_DNA.
EMBL; M19985; AAA60046.1; JOINED; Genomic_DNA.
EMBL; M19986; AAA60046.1; JOINED; Genomic_DNA.
EMBL; M19987; AAA60046.1; JOINED; Genomic_DNA.
EMBL; M19989; AAA60047.1; -; Genomic_DNA.
EMBL; M21571; AAA60047.1; JOINED; Genomic_DNA.
EMBL; M19984; AAA60047.1; JOINED; Genomic_DNA.
EMBL; M19985; AAA60047.1; JOINED; Genomic_DNA.
EMBL; M19986; AAA60047.1; JOINED; Genomic_DNA.
EMBL; M19987; AAA60047.1; JOINED; Genomic_DNA.
EMBL; AB451309; BAG70123.1; -; mRNA.
EMBL; AB451439; BAG70253.1; -; mRNA.
EMBL; AC147651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S62078; AAB26566.1; -; Genomic_DNA.
CCDS; CCDS34578.1; -. [P04085-1]
CCDS; CCDS47524.1; -. [P04085-2]
PIR; A28964; PFHUG1.
PIR; B28964; B28964.
RefSeq; NP_002598.4; NM_002607.5. [P04085-1]
RefSeq; NP_148983.1; NM_033023.4. [P04085-2]
UniGene; Hs.535898; -.
PDB; 3MJK; X-ray; 2.40 A; A/B/E/F/X/Y=21-181.
PDBsum; 3MJK; -.
ProteinModelPortal; P04085; -.
SMR; P04085; -.
BioGrid; 111180; 14.
ComplexPortal; CPX-1874; Platelet-derived growth factor AA complex.
ComplexPortal; CPX-1875; Platelet-derived growth factor AB complex.
ComplexPortal; CPX-2881; PDGF receptor alpha - PDGF-AA complex.
ComplexPortal; CPX-2885; PDGF receptor alpha - PDGF-AB complex.
ComplexPortal; CPX-2886; PDGF receptor beta - PDGF-AB complex.
ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex.
DIP; DIP-5735N; -.
IntAct; P04085; 8.
STRING; 9606.ENSP00000346508; -.
BindingDB; P04085; -.
ChEMBL; CHEMBL3137294; -.
iPTMnet; P04085; -.
PhosphoSitePlus; P04085; -.
BioMuta; PDGFA; -.
EPD; P04085; -.
PaxDb; P04085; -.
PeptideAtlas; P04085; -.
PRIDE; P04085; -.
ProteomicsDB; 51650; -.
ProteomicsDB; 51651; -. [P04085-2]
DNASU; 5154; -.
Ensembl; ENST00000354513; ENSP00000346508; ENSG00000197461. [P04085-1]
Ensembl; ENST00000402802; ENSP00000383889; ENSG00000197461. [P04085-2]
GeneID; 5154; -.
KEGG; hsa:5154; -.
UCSC; uc003sir.4; human. [P04085-1]
CTD; 5154; -.
DisGeNET; 5154; -.
EuPathDB; HostDB:ENSG00000197461.13; -.
GeneCards; PDGFA; -.
H-InvDB; HIX0167622; -.
HGNC; HGNC:8799; PDGFA.
HPA; CAB005579; -.
MIM; 173430; gene.
neXtProt; NX_P04085; -.
OpenTargets; ENSG00000197461; -.
PharmGKB; PA33144; -.
eggNOG; ENOG410IEXJ; Eukaryota.
eggNOG; ENOG4111GMH; LUCA.
GeneTree; ENSGT00510000046755; -.
HOGENOM; HOG000286027; -.
HOVERGEN; HBG053546; -.
InParanoid; P04085; -.
KO; K04359; -.
OMA; MRTWACL; -.
OrthoDB; EOG091G0LNU; -.
PhylomeDB; P04085; -.
TreeFam; TF319554; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; P04085; -.
SIGNOR; P04085; -.
EvolutionaryTrace; P04085; -.
GeneWiki; PDGFA; -.
GenomeRNAi; 5154; -.
PRO; PR:P04085; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000197461; Expressed in 224 organ(s), highest expression level in left coronary artery.
CleanEx; HS_PDGFA; -.
ExpressionAtlas; P04085; baseline and differential.
Genevisible; P04085; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005902; C:microvillus; ISS:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005518; F:collagen binding; IDA:MGI.
GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0048407; F:platelet-derived growth factor binding; IPI:BHF-UCL.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; ISS:UniProtKB.
GO; GO:0001775; P:cell activation; TAS:BHF-UCL.
GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:1990401; P:embryonic lung development; ISS:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0050919; P:negative chemotaxis; IDA:BHF-UCL.
GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; IDA:BHF-UCL.
GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:BHF-UCL.
GO; GO:0060683; P:regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling; ISS:UniProtKB.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
GO; GO:0043588; P:skin development; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; TAS:BHF-UCL.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR006782; PDGF_N.
Pfam; PF00341; PDGF; 1.
Pfam; PF04692; PDGF_N; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complete proteome;
Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
Mitogen; Reference proteome; Secreted; Signal.
SIGNAL 1 20
PROPEP 21 86 Removed in mature form.
/FTId=PRO_0000023356.
CHAIN 87 211 Platelet-derived growth factor subunit A.
/FTId=PRO_0000023357.
REGION 158 162 Receptor binding site. {ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 96 140 {ECO:0000269|PubMed:20534510}.
DISULFID 123 123 Interchain.
{ECO:0000269|PubMed:20534510}.
DISULFID 129 177 {ECO:0000269|PubMed:20534510}.
DISULFID 132 132 Interchain.
{ECO:0000269|PubMed:20534510}.
DISULFID 133 179 {ECO:0000269|PubMed:20534510}.
VAR_SEQ 194 196 GRP -> DVR (in isoform Short).
{ECO:0000303|PubMed:19054851}.
/FTId=VSP_004602.
VAR_SEQ 197 211 Missing (in isoform Short).
{ECO:0000303|PubMed:19054851}.
/FTId=VSP_004603.
CONFLICT 64 66 RAH -> TRD (in Ref. 2; AAA60045).
{ECO:0000305}.
HELIX 27 34 {ECO:0000244|PDB:3MJK}.
HELIX 41 47 {ECO:0000244|PDB:3MJK}.
STRAND 96 104 {ECO:0000244|PDB:3MJK}.
HELIX 107 109 {ECO:0000244|PDB:3MJK}.
STRAND 118 130 {ECO:0000244|PDB:3MJK}.
STRAND 134 181 {ECO:0000244|PDB:3MJK}.
SEQUENCE 211 AA; 24043 MW; 48633DDE558EFA43 CRC64;
MRTLACLLLL GCGYLAHVLA EEAEIPREVI ERLARSQIHS IRDLQRLLEI DSVGSEDSLD
TSLRAHGVHA TKHVPEKRPL PIRRKRSIEE AVPAVCKTRT VIYEIPRSQV DPTSANFLIW
PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV KVAKVEYVRK KPKLKEVQVR LEEHLECACA
TTSLNPDYRE EDTGRPRESG KKRKRKRLKP T


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E0633h ELISA Homo sapiens,Human,PDGF subunit B,PDGF2,PDGF-2,PDGFB,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogen 96T
U0633h CLIA Homo sapiens,Human,PDGF subunit B,PDGF2,PDGF-2,PDGFB,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene 96T
E0633h ELISA kit Homo sapiens,Human,PDGF subunit B,PDGF2,PDGF-2,PDGFB,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-on 96T
U0112m CLIA Mouse,Mus musculus,PDGF subunit A,PDGF-1,Pdgfa,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0112m ELISA kit Mouse,Mus musculus,PDGF subunit A,PDGF-1,Pdgfa,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0112m ELISA Mouse,Mus musculus,PDGF subunit A,PDGF-1,Pdgfa,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
U0633m CLIA Mouse,Mus musculus,PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene c-Sis 96T
E0633m ELISA Mouse,Mus musculus,PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene c-Si 96T
E0633m ELISA kit Mouse,Mus musculus,PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene 96T
U0112b CLIA Bos taurus,Bovine,PDGF subunit A,PDGFA,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0112b ELISA Bos taurus,Bovine,PDGF subunit A,PDGFA,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0112b ELISA kit Bos taurus,Bovine,PDGF subunit A,PDGFA,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
U0633r CLIA PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Rat,Rattus norvegicus 96T
E0633r ELISA PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Rat,Rattus norvegicus 96T
E0633r ELISA kit PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Rat,Rattus norvegicus 96T
E0633p ELISA kit PDGF subunit B,PDGF-2,PDGFB,Pig,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Sus scrofa 96T


 

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