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Thromboxane A2 receptor (TXA2-R) (Prostanoid TP receptor)

 TA2R_HUMAN              Reviewed;         343 AA.
P21731; O75228; Q6DK52; Q9UCY1; Q9UCY2;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
12-SEP-2018, entry version 193.
RecName: Full=Thromboxane A2 receptor;
Short=TXA2-R;
AltName: Full=Prostanoid TP receptor;
Name=TBXA2R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=1825698; DOI=10.1038/349617a0;
Hirata M., Hayashi Y., Ushikubi F., Yokota Y., Kageyama R.,
Nakanishi S., Narumiya S.;
"Cloning and expression of cDNA for a human thromboxane A2 receptor.";
Nature 349:617-620(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8227091;
Nuesing R.M., Hirata M., Kakizuka A., Eki T., Ozawa K., Narumiya S.;
"Characterization and chromosomal mapping of the human thromboxane A2
receptor gene.";
J. Biol. Chem. 268:25253-25259(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE
SPLICING.
TISSUE=Endothelial cell, and Placenta;
PubMed=8034687;
Raychowdhury M.K., Yukawa M., Collins L.J., McGrail S.H., Kent K.C.,
Ware J.A.;
"Alternative splicing produces a divergent cytoplasmic tail in the
human endothelial thromboxane A2 receptor.";
J. Biol. Chem. 269:19256-19261(1994).
[4]
ERRATUM.
PubMed=7896853; DOI=10.1074/jbc.270.12.7011;
Raychowdhury M.K., Yukawa M., Collins L.J., McGrail S.H., Kent K.C.,
Ware J.A.;
J. Biol. Chem. 270:7011-7011(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7965765;
D'Angelo D.D., Davis M.G., Ali S., Dorn G.W. II;
"Cloning and pharmacologic characterization of a thromboxane A2
receptor from K562 (human chronic myelogenous leukemia) cells.";
J. Pharmacol. Exp. Ther. 271:1034-1041(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 329-343 (ISOFORMS 1 AND 2), FUNCTION,
ALTERNATIVE SPLICING, AND CHARACTERIZATION OF VARIANT BDPLT13 LEU-60.
TISSUE=Platelet;
PubMed=8613548; DOI=10.1172/JCI118518;
Hirata T., Ushikubi F., Kakizuka A., Okuma M., Narumiya S.;
"Two thromboxane A2 receptor isoforms in human platelets. Opposite
coupling to adenylyl cyclase with different sensitivity to Arg60 to
Leu mutation.";
J. Clin. Invest. 97:949-956(1996).
[12]
MUTAGENESIS.
PubMed=8246916;
Funk C.D., Furci L., Moran N., Fitzgerald G.A.;
"Point mutation in the seventh hydrophobic domain of the human
thromboxane A2 receptor allows discrimination between agonist and
antagonist binding sites.";
Mol. Pharmacol. 44:934-939(1993).
[13]
INTERACTION WITH PSMA3.
PubMed=17499743; DOI=10.1016/j.prostaglandins.2006.12.001;
Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S.,
Nakahata N.;
"Low expression of cell-surface thromboxane A2 receptor beta-isoform
through the negative regulation of its membrane traffic by
proteasomes.";
Prostaglandins Other Lipid Mediat. 83:237-249(2007).
[14]
INTERACTION WITH RACK1.
PubMed=18088317; DOI=10.1111/j.1600-0854.2007.00692.x;
Parent A., Laroche G., Hamelin E., Parent J.L.;
"RACK1 regulates the cell surface expression of the G protein-coupled
receptor for thromboxane A(2).";
Traffic 9:394-407(2008).
[15]
INTERACTION WITH RPGRIP1L.
PubMed=19464661; DOI=10.1016/j.prostaglandins.2009.02.001;
Tokue S., Sasaki M., Nakahata N.;
"Thromboxane A2-induced signal transduction is negatively regulated by
KIAA1005 that directly interacts with thromboxane A2 receptor.";
Prostaglandins Other Lipid Mediat. 89:8-15(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
VARIANT BDPLT13 LEU-60, AND CHARACTERIZATION OF VARIANT BDPLT13
LEU-60.
PubMed=7929844; DOI=10.1172/JCI117510;
Hirata T., Kakizuka A., Ushikubi F., Fuse I., Okuma M., Narumiya S.;
"Arg60 to Leu mutation of the human thromboxane A2 receptor in a
dominantly inherited bleeding disorder.";
J. Clin. Invest. 94:1662-1667(1994).
-!- FUNCTION: Receptor for thromboxane A2 (TXA2), a potent stimulator
of platelet aggregation. The activity of this receptor is mediated
by a G-protein that activates a phosphatidylinositol-calcium
second messenger system. In the kidney, the binding of TXA2 to
glomerular TP receptors causes intense vasoconstriction. Activates
phospholipase C. Isoform 1 activates adenylyl cyclase. Isoform 2
inhibits adenylyl cyclase. {ECO:0000269|PubMed:8613548}.
-!- SUBUNIT: Interacts with RPGRIP1L. Interacts with PSMA3. Interacts
with RACK1; the interaction regulates TBXA2R cell surface
expression. {ECO:0000269|PubMed:17499743,
ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:19464661}.
-!- INTERACTION:
Q12791-5:KCNMA1; NbExp=7; IntAct=EBI-15885629, EBI-15861807;
Q13162:PRDX4; NbExp=3; IntAct=EBI-2625082, EBI-2211957;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha;
IsoId=P21731-3; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=P21731-2; Sequence=VSP_001925;
Note=Ref.2 (AAA58957) sequence differs from that shown due to
frameshifts in positions 330 and 386. {ECO:0000305};
-!- DISEASE: Bleeding disorder, platelet-type 13 (BDPLT13)
[MIM:614009]: A disorder characterized by reduced platelet
aggregation and a tendency to mild mucocutaneous bleeding.
{ECO:0000269|PubMed:7929844, ECO:0000269|PubMed:8613548}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=AAA58957.1; Type=Frameshift; Positions=329; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tbxa2r/";
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EMBL; D38081; BAA07274.1; -; mRNA.
EMBL; D15056; BAA03649.1; -; Genomic_DNA.
EMBL; U11271; AAA58957.1; ALT_FRAME; mRNA.
EMBL; U27325; AAA68608.1; -; mRNA.
EMBL; AY429110; AAR07905.1; -; mRNA.
EMBL; DQ268653; ABB72549.1; -; Genomic_DNA.
EMBL; AC005175; AAC24302.1; -; Genomic_DNA.
EMBL; AC005175; AAC24303.1; -; Genomic_DNA.
EMBL; CH471139; EAW69301.1; -; Genomic_DNA.
EMBL; BC074749; AAH74749.1; -; mRNA.
EMBL; BC074750; AAH74750.1; -; mRNA.
CCDS; CCDS42467.1; -. [P21731-3]
CCDS; CCDS54198.1; -. [P21731-2]
PIR; A49117; A49117.
PIR; A53959; A53959.
PIR; A56194; A56194.
PIR; T02670; T02670.
RefSeq; NP_001051.1; NM_001060.5. [P21731-3]
RefSeq; NP_963998.2; NM_201636.2. [P21731-2]
RefSeq; XP_011526516.1; XM_011528214.2. [P21731-3]
UniGene; Hs.442530; -.
PDB; 1LBN; Model; -; A=100-265.
PDBsum; 1LBN; -.
ProteinModelPortal; P21731; -.
BioGrid; 112777; 53.
DIP; DIP-41465N; -.
IntAct; P21731; 6.
MINT; P21731; -.
STRING; 9606.ENSP00000393333; -.
BindingDB; P21731; -.
ChEMBL; CHEMBL2069; -.
DrugBank; DB01207; Ridogrel.
GuidetoPHARMACOLOGY; 346; -.
iPTMnet; P21731; -.
PhosphoSitePlus; P21731; -.
SwissPalm; P21731; -.
BioMuta; TBXA2R; -.
DMDM; 229463010; -.
PaxDb; P21731; -.
PeptideAtlas; P21731; -.
PRIDE; P21731; -.
ProteomicsDB; 53894; -.
ProteomicsDB; 53895; -. [P21731-2]
Ensembl; ENST00000375190; ENSP00000364336; ENSG00000006638. [P21731-3]
Ensembl; ENST00000411851; ENSP00000393333; ENSG00000006638. [P21731-2]
GeneID; 6915; -.
KEGG; hsa:6915; -.
UCSC; uc002lyg.3; human. [P21731-3]
CTD; 6915; -.
DisGeNET; 6915; -.
EuPathDB; HostDB:ENSG00000006638.11; -.
GeneCards; TBXA2R; -.
H-InvDB; HIX0202922; -.
HGNC; HGNC:11608; TBXA2R.
HPA; HPA077366; -.
MalaCards; TBXA2R; -.
MIM; 188070; gene.
MIM; 614009; phenotype.
neXtProt; NX_P21731; -.
OpenTargets; ENSG00000006638; -.
Orphanet; 220443; Bleeding diathesis due to thromboxane synthesis deficiency.
PharmGKB; PA348; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000119188; -.
HOGENOM; HOG000015238; -.
HOVERGEN; HBG108543; -.
InParanoid; P21731; -.
KO; K04264; -.
OMA; RVYHDRE; -.
OrthoDB; EOG091G0DNT; -.
PhylomeDB; P21731; -.
TreeFam; TF324982; -.
Reactome; R-HSA-391908; Prostanoid ligand receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
SignaLink; P21731; -.
SIGNOR; P21731; -.
ChiTaRS; TBXA2R; human.
GeneWiki; Thromboxane_receptor; -.
GenomeRNAi; 6915; -.
PRO; PR:P21731; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000006638; Expressed in 206 organ(s), highest expression level in metanephric glomerulus.
CleanEx; HS_TBXA2R; -.
ExpressionAtlas; P21731; baseline and differential.
Genevisible; P21731; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004961; F:thromboxane A2 receptor activity; TAS:ProtInc.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IGI:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
GO; GO:0045777; P:positive regulation of blood pressure; IBA:GO_Central.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0019932; P:second-messenger-mediated signaling; IEA:Ensembl.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR008365; Prostanoid_rcpt.
InterPro; IPR001105; Thbox_rcpt.
PANTHER; PTHR11866; PTHR11866; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01788; PROSTANOIDR.
PRINTS; PR00429; THROMBOXANER.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 343 Thromboxane A2 receptor.
/FTId=PRO_0000070138.
TOPO_DOM 1 29 Extracellular. {ECO:0000255}.
TRANSMEM 30 52 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 53 66 Cytoplasmic. {ECO:0000255}.
TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 88 106 Extracellular. {ECO:0000255}.
TRANSMEM 107 128 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 129 149 Cytoplasmic. {ECO:0000255}.
TRANSMEM 150 172 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 173 193 Extracellular. {ECO:0000255}.
TRANSMEM 194 219 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 220 246 Cytoplasmic. {ECO:0000255}.
TRANSMEM 247 270 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 271 289 Extracellular. {ECO:0000255}.
TRANSMEM 290 311 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 312 343 Cytoplasmic. {ECO:0000255}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000250|UniProtKB:P30987}.
CARBOHYD 4 4 N-linked (GlcNAc...) asparagine.
CARBOHYD 16 16 N-linked (GlcNAc...) asparagine.
DISULFID 105 183 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 329 343 SLSLQPQLTQRSGLQ -> RSLTLWPSLEYSGTISAHCNLR
LPGSSDSRASASRAAGITGVSHCARPCMLFDPEFDLLAGVQ
LLPFEPPTGKALSRKD (in isoform 2).
{ECO:0000303|PubMed:8034687,
ECO:0000303|PubMed:8613548}.
/FTId=VSP_001925.
VARIANT 60 60 R -> L (in BDPLT13; does not affect TXA2
binding; defective interaction with G
proteins; impairs phospholipase C and
adenylyl cyclase activation; isoform 1;
has no effect on adenylyl cyclase
inhibition; isoform 2; dbSNP:rs34377097).
{ECO:0000269|PubMed:7929844,
ECO:0000269|PubMed:8613548}.
/FTId=VAR_003515.
VARIANT 68 68 C -> S (in dbSNP:rs5743).
/FTId=VAR_014688.
VARIANT 80 80 V -> E (in dbSNP:rs5744).
/FTId=VAR_014689.
VARIANT 94 94 E -> V (in dbSNP:rs5746).
/FTId=VAR_014690.
VARIANT 160 160 A -> T (in dbSNP:rs5749).
/FTId=VAR_014691.
VARIANT 176 176 V -> E (in dbSNP:rs5750).
/FTId=VAR_014692.
VARIANT 217 217 V -> I (in dbSNP:rs5751).
/FTId=VAR_014693.
MUTAGEN 291 291 L->R: Suppresses antagonist binding.
{ECO:0000269|PubMed:8246916}.
MUTAGEN 295 295 R->Q: Reduces antagonist binding.
{ECO:0000269|PubMed:8246916}.
MUTAGEN 299 299 W->L: Reduces antagonist binding.
{ECO:0000269|PubMed:8246916}.
MUTAGEN 299 299 W->R: Reduces antagonist binding.
{ECO:0000269|PubMed:8246916}.
CONFLICT 263 263 V -> W (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 343 AA; 37431 MW; 114A7C3F3F0D35F1 CRC64;
MWPNGSSLGP CFRPTNITLE ERRLIASPWF AASFCVVGLA SNLLALSVLA GARQGGSHTR
SSFLTFLCGL VLTDFLGLLV TGTIVVSQHA ALFEWHAVDP GCRLCRFMGV VMIFFGLSPL
LLGAAMASER YLGITRPFSR PAVASQRRAW ATVGLVWAAA LALGLLPLLG VGRYTVQYPG
SWCFLTLGAE SGDVAFGLLF SMLGGLSVGL SFLLNTVSVA TLCHVYHGQE AAQQRPRDSE
VEMMAQLLGI MVVASVCWLP LLVFIAQTVL RNPPAMSPAG QLSRTTEKEL LIYLRVATWN
QILDPWVYIL FRRAVLRRLQ PRLSTRPRSL SLQPQLTQRS GLQ


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E0749m ELISA kit Mouse,Mus musculus,PGF receptor,PGF2-alpha receptor,Prostaglandin F2-alpha receptor,Prostanoid FP receptor,Ptgfr 96T
E0749b ELISA kit Bos taurus,Bovine,PGF receptor,PGF2-alpha receptor,Prostaglandin F2-alpha receptor,Prostanoid FP receptor,PTGFR 96T
U0749r CLIA PGF receptor,PGF2-alpha receptor,Prostaglandin F2-alpha receptor,Prostanoid FP receptor,Ptgfr,Rat,Rattus norvegicus 96T
E0749r ELISA kit PGF receptor,PGF2-alpha receptor,Prostaglandin F2-alpha receptor,Prostanoid FP receptor,Ptgfr,Rat,Rattus norvegicus 96T


 

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