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Platelet-derived growth factor D (PDGF-D) (Spinal cord-derived growth factor B) (SCDGF-B) [Cleaved into: Platelet-derived growth factor D, latent form (PDGFD latent form); Platelet-derived growth factor D, receptor-binding form (PDGFD receptor-binding form)]
PDGFD_MOUSE Reviewed; 370 AA.
Q925I7; Q3URF6; Q8K2L3; Q9D1L8;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
28-FEB-2018, entry version 119.
RecName: Full=Platelet-derived growth factor D;
Short=PDGF-D;
AltName: Full=Spinal cord-derived growth factor B;
Short=SCDGF-B;
Contains:
RecName: Full=Platelet-derived growth factor D, latent form;
Short=PDGFD latent form;
Contains:
RecName: Full=Platelet-derived growth factor D, receptor-binding form;
Short=PDGFD receptor-binding form;
Flags: Precursor;
Name=Pdgfd; Synonyms=Scdgfb;
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).
STRAIN=BALB/cJ;
PubMed=11331882; DOI=10.1038/35074593;
LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A.,
Giese N.A., Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C.,
Burgess C.E., Fernandez E., Deegler L.L., Rittman B., Shimkets J.,
Shimkets R.A., Rothberg J.M., Lichenstein H.S.;
"PDGF D, a novel protease-activated growth factor.";
Nat. Cell Biol. 3:517-521(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
PubMed=12890490; DOI=10.1016/S0006-291X(03)01346-9;
Zhuo Y., Hoyle G.W., Zhang J., Morris G., Lasky J.A.;
"A novel murine PDGF-D splicing variant results in significant
differences in peptide expression and function.";
Biochem. Biophys. Res. Commun. 308:126-132(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[5]
TISSUE SPECIFICITY.
PubMed=11331881; DOI=10.1038/35074588;
Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H.,
Alitalo K., Eriksson U.;
"PDGF-D is a specific, protease-activated ligand for the PDGF beta-
receptor.";
Nat. Cell Biol. 3:512-516(2001).
[6]
FUNCTION.
PubMed=11980634;
LaRochelle W.J., Jeffers M., Corvalan J.R.F., Jia X.-C., Feng X.,
Vanegas S., Vickroy J.D., Yang X.-D., Chen F., Gazit G., Mayotte J.,
Macaluso J., Rittman B., Wu F., Dhanabal M., Herrmann J.,
Lichenstein H.S.;
"Platelet-derived growth factor D: tumorigenicity in mice and
dysregulated expression in human cancer.";
Cancer Res. 62:2468-2473(2002).
[7]
REVIEW.
PubMed=15207812; DOI=10.1016/j.cytogfr.2004.03.003;
Tallquist M., Kazlauskas A.;
"PDGF signaling in cells and mice.";
Cytokine Growth Factor Rev. 15:205-213(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14747375; DOI=10.1097/01.ASN.0000108522.79652.63;
Hudkins K.L., Gilbertson D.G., Carling M., Taneda S., Hughes S.D.,
Holdren M.S., Palmer T.E., Topouzis S., Haran A.C., Feldhaus A.L.,
Alpers C.E.;
"Exogenous PDGF-D is a potent mesangial cell mitogen and causes a
severe mesangial proliferative glomerulopathy.";
J. Am. Soc. Nephrol. 15:286-298(2004).
[9]
TISSUE SPECIFICITY.
PubMed=14514732; DOI=10.1097/01.ASN.0000089828.73014.C8;
Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G.,
Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E.;
"Obstructive uropathy in mice and humans: potential role for PDGF-D in
the progression of tubulointerstitial injury.";
J. Am. Soc. Nephrol. 14:2544-2555(2003).
[10]
FUNCTION.
PubMed=15271796; DOI=10.1182/blood-2004-04-1485;
Uutela M., Wirzenius M., Paavonen K., Rajantie I., He Y., Karpanen T.,
Lohela M., Wiig H., Salven P., Pajusola K., Eriksson U., Alitalo K.;
"PDGF-D induces macrophage recruitment, increased interstitial
pressure, and blood vessel maturation during angiogenesis.";
Blood 104:3198-3204(2004).
-!- 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. Plays an important role in wound healing (By
similarity). Has oncogenic potential and can induce tumor
formation. Induces macrophage recruitment, increased interstitial
pressure, and blood vessel maturation during angiogenesis. Can
initiate events that lead to a mesangial proliferative
glomerulonephritis, including influx of monocytes and macrophages
and production of extracellular matrix. {ECO:0000250,
ECO:0000269|PubMed:11980634, ECO:0000269|PubMed:14747375,
ECO:0000269|PubMed:15271796}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB
homodimers, and with heterodimers formed by PDGFRA and PDGFRB (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released by
platelets upon wounding. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=Q925I7-1; Sequence=Displayed;
Name=2;
IsoId=Q925I7-2; Sequence=VSP_020616;
Name=3; Synonyms=Short;
IsoId=Q925I7-3; Sequence=VSP_020617, VSP_020618;
-!- TISSUE SPECIFICITY: Expressed at high levels in developing heart,
lung, kidney and some muscle derivatives. Moderately expressed in
liver, brain and testis. In the kidney, localized to glomerular
mesangial cells and vascular smooth muscle cells. Up-regulated in
areas of renal fibrosis. In mice with unilateral ureteral
obstruction, expressed in interstitial cells at day 4, with an
increased to maximal expression at day 14.
{ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:12890490,
ECO:0000269|PubMed:14514732, ECO:0000269|PubMed:14747375}.
-!- PTM: Activated by proteolytic cleavage. Proteolytic removal of the
N-terminal CUB domain releasing the core domain is necessary for
unmasking the receptor-binding epitopes of the core domain.
Cleavage after Arg-247 or Arg-249 by urokinase plasminogen
activator gives rise to the active form (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF335583; AAK38839.1; -; mRNA.
EMBL; AK003359; BAB22735.2; -; mRNA.
EMBL; AK141551; BAE24732.1; -; mRNA.
EMBL; BC030896; AAH30896.1; -; mRNA.
CCDS; CCDS22801.1; -. [Q925I7-1]
RefSeq; NP_082200.1; NM_027924.2. [Q925I7-1]
RefSeq; XP_006509948.1; XM_006509885.3.
RefSeq; XP_006509949.1; XM_006509886.3.
UniGene; Mm.390122; -.
ProteinModelPortal; Q925I7; -.
SMR; Q925I7; -.
STRING; 10090.ENSMUSP00000128388; -.
PhosphoSitePlus; Q925I7; -.
PaxDb; Q925I7; -.
PeptideAtlas; Q925I7; -.
PRIDE; Q925I7; -.
Ensembl; ENSMUST00000058692; ENSMUSP00000056240; ENSMUSG00000032006. [Q925I7-2]
Ensembl; ENSMUST00000168039; ENSMUSP00000128388; ENSMUSG00000032006. [Q925I7-1]
Ensembl; ENSMUST00000214892; ENSMUSP00000149162; ENSMUSG00000032006. [Q925I7-3]
GeneID; 71785; -.
KEGG; mmu:71785; -.
UCSC; uc009oby.1; mouse. [Q925I7-1]
UCSC; uc009obz.1; mouse. [Q925I7-2]
UCSC; uc012gnq.1; mouse. [Q925I7-3]
CTD; 80310; -.
MGI; MGI:1919035; Pdgfd.
eggNOG; ENOG410IGUN; Eukaryota.
eggNOG; ENOG41106HA; LUCA.
GeneTree; ENSGT00390000005171; -.
HOGENOM; HOG000261610; -.
HOVERGEN; HBG057324; -.
InParanoid; Q925I7; -.
KO; K05450; -.
OMA; YHSPSVT; -.
OrthoDB; EOG091G08SH; -.
PhylomeDB; Q925I7; -.
TreeFam; TF332130; -.
Reactome; R-MMU-186797; Signaling by PDGF.
PRO; PR:Q925I7; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032006; -.
CleanEx; MM_PDGFD; -.
Genevisible; Q925I7; MM.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
GO; GO:0009987; P:cellular process; ISO:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:2000439; P:positive regulation of monocyte extravasation; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
CDD; cd00041; CUB; 1.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR027123; PDGFD.
InterPro; IPR035914; Sperma_CUB_dom_sf.
PANTHER; PTHR11633:SF4; PTHR11633:SF4; 1.
Pfam; PF00431; CUB; 1.
Pfam; PF00341; PDGF; 1.
SMART; SM00042; CUB; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS50278; PDGF_2; 1.
2: Evidence at transcript level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Growth factor; Mitogen; Proto-oncogene;
Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 370 Platelet-derived growth factor D, latent
form.
/FTId=PRO_0000250190.
CHAIN 250 370 Platelet-derived growth factor D,
receptor-binding form. {ECO:0000255}.
/FTId=PRO_0000250191.
DOMAIN 52 170 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
SITE 247 248 Cleavage. {ECO:0000255}.
SITE 249 250 Cleavage. {ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 109 131 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 296 296 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DISULFID 302 360 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 306 362 {ECO:0000255|PROSITE-ProRule:PRU00059}.
VAR_SEQ 42 47 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020616.
VAR_SEQ 258 261 VDLD -> GIEV (in isoform 3).
{ECO:0000303|PubMed:12890490,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020617.
VAR_SEQ 262 370 Missing (in isoform 3).
{ECO:0000303|PubMed:12890490,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020618.
CONFLICT 173 173 F -> S (in Ref. 4; AAH30896).
{ECO:0000305}.
SEQUENCE 370 AA; 42809 MW; 9E80B4CF6813BFBE CRC64;
MQRLVLVSIL LCANFSCYPD TFATPQRASI KALRNANLRR DESNHLTDLY QREENIQVTS
NGHVQSPRFP NSYPRNLLLT WWLRSQEKTR IQLSFDHQFG LEEAENDICR YDFVEVEEVS
ESSTVVRGRW CGHKEIPPRI TSRTNQIKIT FKSDDYFVAK PGFKIYYSFV EDFQPEAASE
TNWESVTSSF SGVSYHSPSI TDPTLTADAL DKTVAEFDTV EDLLKHFNPV SWQDDLENLY
LDTPHYRGRS YHDRKSKVDL DRLNDDVKRY SCTPRNHSVN LREELKLTNA VFFPRCLLVQ
RCGGNCGCGT VNWKSCTCSS GKTVKKYHEV LKFEPGHFKR RGKAKNMALV DIQLDHHERC
DCICSSRPPR
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Pathways :
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP2148: Brain derived neurotrophic factor
WP474: Endochondral Ossification
WP1065: Endochondral Ossification
WP1181: Endochondral Ossification
WP1270: Endochondral Ossification
WP1308: Endochondral Ossification
WP1869: Neuroransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
WP1983: Splicing factor NOVA regulated synpatic proteins
WP2256: Integrated Pancreatic Cancer Pathway
WP2292: Chemokine signaling pathway
WP2377: Integrated Pancreatic Cancer Pathway
WP828: Endochondral Ossification
WP947: Endochondral Ossification
Related Genes :
[PDGFRA PDGFR2 RHEPDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[PDGFC SCDGF UNQ174/PRO200] Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (SCDGF) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)]
[Pdgfc Scdgf] Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (SCDGF) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)]
[PDGFD IEGF SCDGFB MSTP036 UNQ1899/PRO4345] Platelet-derived growth factor D (PDGF-D) (Iris-expressed growth factor) (Spinal cord-derived growth factor B) (SCDGF-B) [Cleaved into: Platelet-derived growth factor D, latent form (PDGFD latent form); Platelet-derived growth factor D, receptor-binding form (PDGFD receptor-binding form)]
[Pdgfd Scdgfb] Platelet-derived growth factor D (PDGF-D) (Spinal cord-derived growth factor B) (SCDGF-B) [Cleaved into: Platelet-derived growth factor D, latent form (PDGFD latent form); Platelet-derived growth factor D, receptor-binding form (PDGFD receptor-binding form)]
[Pdgfc Scdgf] Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (rScdfg) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)]
[Pdgfd Iegf Scdgfb] Platelet-derived growth factor D (PDGF-D) (Iris-expressed growth factor) (Spinal cord-derived growth factor B) (SCDGF-B) [Cleaved into: Platelet-derived growth factor D, latent form (PDGFD latent form); Platelet-derived growth factor D, receptor-binding form (PDGFD receptor-binding form)]
[PDGFB PDGF2 SIS] Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis) (Becaplermin)
[PDGFA PDGF1] Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)
[PDGFC SCDGF] Platelet-derived growth factor C (PDGF-C) (Spinal cord-derived growth factor) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)]
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Pdgfb Sis] Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis)
[Pdgfa Rpa1] Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)
[Pdgfb] Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Fragment)
[Pdgfa] Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)
[PDGFB] Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide)
[pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFA] Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)
[PDGFB SIS] Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis)
[PDGFB] Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PPBP CTAP3 CXCL7 SCYB7 TGB1 THBGB1] Platelet basic protein (PBP) (C-X-C motif chemokine 7) (Leukocyte-derived growth factor) (LDGF) (Macrophage-derived growth factor) (MDGF) (Small-inducible cytokine B7) [Cleaved into: Connective tissue-activating peptide III (CTAP-III) (LA-PF4) (Low-affinity platelet factor IV); TC-2; Connective tissue-activating peptide III(1-81) (CTAP-III(1-81)); Beta-thromboglobulin (Beta-TG); Neutrophil-activating peptide 2(74) (NAP-2(74)); Neutrophil-activating peptide 2(73) (NAP-2(73)); Neutrophil-activating peptide 2 (NAP-2); TC-1; Neutrophil-activating peptide 2(1-66) (NAP-2(1-66)); Neutrophil-activating peptide 2(1-63) (NAP-2(1-63))]
[PDGFA] Platelet-derived growth factor subunit A (PDGF subunit A) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
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