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Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase)

 PTGIS_HUMAN             Reviewed;         500 AA.
Q16647; Q3MII8; Q9HAX2; Q9HAX3; Q9HAX4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 172.
RecName: Full=Prostacyclin synthase;
EC=5.3.99.4 {ECO:0000269|PubMed:18032380, ECO:0000269|PubMed:25623425};
AltName: Full=Prostaglandin I2 synthase;
Name=PTGIS; Synonyms=CYP8, CYP8A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aorta;
PubMed=8185632; DOI=10.1006/bbrc.1994.1652;
Miyata A., Hara S., Yokoyama C., Inoue H., Ullrich V., Tanabe T.;
"Molecular cloning and expression of human prostacyclin synthase.";
Biochem. Biophys. Res. Commun. 200:1728-1734(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-38; ARG-118 AND SER-379.
PubMed=11281454; DOI=10.1007/s004390000444;
Chevalier D., Cauffiez C., Bernard C., Lo-Guidice J.-M., Allorge D.,
Fazio F., Ferrari N., Libersa C., Lhermitte M., D'Halluin J.C.,
Broly F.;
"Characterization of new mutations in the coding sequence and 5'-
untranslated region of the human prostacyclin synthase gene
(CYP8A1).";
Hum. Genet. 108:148-155(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
INVOLVEMENT IN EHT.
PubMed=12372404; DOI=10.1016/S0006-291X(02)02341-0;
Nakayama T., Soma M., Watanabe Y., Hasimu B., Sato M., Aoi N.,
Kosuge K., Kanmatsuse K., Kokubun S., Marrow J.D., Oates J.A.;
"Splicing mutation of the prostacyclin synthase gene in a family
associated with hypertension.";
Biochem. Biophys. Res. Commun. 297:1135-1139(2002).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT
THR-447, AND CHARACTERIZATION OF VARIANT THR-447.
PubMed=25623425; DOI=10.1016/j.abb.2015.01.012;
Cho S.A., Rohn-Glowacki K.J., Jarrar Y.B., Yi M., Kim W.Y., Shin J.G.,
Lee S.J.;
"Analysis of genetic polymorphism and biochemical characterization of
a functionally decreased variant in prostacyclin synthase gene
(CYP8A1) in humans.";
Arch. Biochem. Biophys. 569C:10-18(2015).
[7]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 23-500 IN COMPLEX WITH HEME,
AND COFACTOR.
PubMed=17020766; DOI=10.1016/j.jmb.2006.09.039;
Chiang C.W., Yeh H.C., Wang L.H., Chan N.L.;
"Crystal structure of the human prostacyclin synthase.";
J. Mol. Biol. 364:266-274(2006).
[8]
X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 18-500 IN COMPLEX WITH HEME
AND INHIBITOR MINOXIDIL, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18032380; DOI=10.1074/jbc.M707470200;
Li Y.C., Chiang C.W., Yeh H.C., Hsu P.Y., Whitby F.G., Wang L.H.,
Chan N.L.;
"Structures of prostacyclin synthase and its complexes with substrate
analog and inhibitor reveal a ligand-specific heme conformation
change.";
J. Biol. Chem. 283:2917-2926(2008).
-!- FUNCTION: Catalyzes the isomerization of prostaglandin H2 to
prostacyclin (= prostaglandin I2). {ECO:0000269|PubMed:18032380,
ECO:0000269|PubMed:25623425}.
-!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-6,9-alpha-epoxy-11-
alpha,15-dihydroxyprosta-5,13-dienoate.
{ECO:0000269|PubMed:18032380, ECO:0000269|PubMed:25623425}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:17020766,
ECO:0000269|PubMed:18032380};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.55 uM for 6-keto-PGF1alpha {ECO:0000269|PubMed:25623425};
KM=13 uM for prostaglandin H2 (at 23 degrees Celsius)
{ECO:0000269|PubMed:18032380};
Vmax=534 mmol/min/pg enzyme {ECO:0000269|PubMed:25623425};
Vmax=980 mol/min/mol enzyme {ECO:0000269|PubMed:18032380};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q29626}; Single-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Widely expressed; particularly abundant in
ovary, heart, skeletal muscle, lung and prostate.
-!- DISEASE: Essential hypertension (EHT) [MIM:145500]: A condition in
which blood pressure is consistently higher than normal with no
identifiable cause. {ECO:0000269|PubMed:12372404}. Note=The
disease may be caused by mutations affecting the gene represented
in this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
Note=CYP8A1 alleles;
URL="http://www.cypalleles.ki.se/cyp8a1.htm";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTGISID44219ch20q13.html";
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EMBL; D38145; BAA07343.1; -; mRNA.
EMBL; AF297048; AAG31781.1; -; mRNA.
EMBL; AF297049; AAG31782.1; -; mRNA.
EMBL; AF297050; AAG31783.1; -; mRNA.
EMBL; AF297051; AAG31784.1; -; mRNA.
EMBL; AF297052; AAG31785.1; -; mRNA.
EMBL; AL118525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC101809; AAI01810.1; -; mRNA.
EMBL; BC101811; AAI01812.1; -; mRNA.
CCDS; CCDS13419.1; -.
PIR; JC2231; JC2231.
RefSeq; NP_000952.1; NM_000961.3.
UniGene; Hs.302085; -.
PDB; 2IAG; X-ray; 2.15 A; A/B=23-500.
PDB; 3B6H; X-ray; 1.62 A; A/B=18-500.
PDBsum; 2IAG; -.
PDBsum; 3B6H; -.
ProteinModelPortal; Q16647; -.
SMR; Q16647; -.
BioGrid; 111712; 4.
STRING; 9606.ENSP00000244043; -.
BindingDB; Q16647; -.
ChEMBL; CHEMBL4428; -.
DrugBank; DB01240; Epoprostenol.
DrugBank; DB00812; Phenylbutazone.
GuidetoPHARMACOLOGY; 1356; -.
SwissLipids; SLP:000001097; -.
iPTMnet; Q16647; -.
PhosphoSitePlus; Q16647; -.
BioMuta; PTGIS; -.
DMDM; 2493373; -.
EPD; Q16647; -.
MaxQB; Q16647; -.
PaxDb; Q16647; -.
PeptideAtlas; Q16647; -.
PRIDE; Q16647; -.
Ensembl; ENST00000244043; ENSP00000244043; ENSG00000124212.
GeneID; 5740; -.
KEGG; hsa:5740; -.
UCSC; uc002xut.4; human.
CTD; 5740; -.
DisGeNET; 5740; -.
EuPathDB; HostDB:ENSG00000124212.5; -.
GeneCards; PTGIS; -.
HGNC; HGNC:9603; PTGIS.
HPA; CAB009517; -.
HPA; HPA014193; -.
MalaCards; PTGIS; -.
MIM; 145500; phenotype.
MIM; 601699; gene.
neXtProt; NX_Q16647; -.
OpenTargets; ENSG00000124212; -.
PharmGKB; PA292; -.
eggNOG; KOG0684; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00550000074551; -.
HOVERGEN; HBG051100; -.
InParanoid; Q16647; -.
KO; K01831; -.
OMA; VFHTFRQ; -.
OrthoDB; EOG091G0767; -.
PhylomeDB; Q16647; -.
TreeFam; TF105090; -.
BioCyc; MetaCyc:HS04738-MONOMER; -.
BRENDA; 5.3.99.4; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-197264; Nicotinamide salvaging.
Reactome; R-HSA-211979; Eicosanoids.
Reactome; R-HSA-211994; Sterols are 12-hydroxylated by CYP8B1.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
EvolutionaryTrace; Q16647; -.
GeneWiki; Prostacyclin_synthase; -.
GenomeRNAi; 5740; -.
PRO; PR:Q16647; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124212; -.
CleanEx; HS_PTGIS; -.
Genevisible; Q16647; HS.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
GO; GO:0008116; F:prostaglandin-I synthase activity; IDA:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:UniProtKB.
GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0006690; P:icosanoid metabolic process; TAS:Reactome.
GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR024204; Cyt_P450_CYP7A1-type.
InterPro; IPR002403; Cyt_P450_E_grp-IV.
InterPro; IPR036396; Cyt_P450_sf.
InterPro; IPR027286; PTGIS.
PANTHER; PTHR24306:SF4; PTHR24306:SF4; 1.
Pfam; PF00067; p450; 1.
PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
PIRSF; PIRSF500628; PTGIS; 1.
PRINTS; PR00465; EP450IV.
SUPFAM; SSF48264; SSF48264; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron; Isomerase;
Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
Polymorphism; Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 500 Prostacyclin synthase.
/FTId=PRO_0000051910.
TRANSMEM 1 20 Helical. {ECO:0000255}.
REGION 358 359 Substrate binding.
{ECO:0000250|UniProtKB:F1RE08}.
METAL 441 441 Iron (heme axial ligand).
{ECO:0000244|PDB:2IAG,
ECO:0000244|PDB:3B6H,
ECO:0000269|PubMed:17020766,
ECO:0000269|PubMed:18032380}.
BINDING 106 106 Substrate.
{ECO:0000250|UniProtKB:F1RE08}.
BINDING 112 112 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:F1RE08}.
BINDING 287 287 Substrate.
{ECO:0000250|UniProtKB:F1RE08}.
BINDING 382 382 Substrate.
{ECO:0000250|UniProtKB:F1RE08}.
VARIANT 38 38 P -> L (in allele CYP8A1*2).
{ECO:0000269|PubMed:11281454}.
/FTId=VAR_010915.
VARIANT 118 118 S -> R (in allele CYP8A1*3;
dbSNP:rs5622).
{ECO:0000269|PubMed:11281454}.
/FTId=VAR_010916.
VARIANT 154 154 E -> A (in dbSNP:rs5623).
/FTId=VAR_014634.
VARIANT 171 171 F -> L (in dbSNP:rs5624).
/FTId=VAR_014635.
VARIANT 236 236 R -> C (in dbSNP:rs5626).
/FTId=VAR_014636.
VARIANT 379 379 R -> S (in allele CYP8A1*4;
dbSNP:rs56195291).
{ECO:0000269|PubMed:11281454}.
/FTId=VAR_010917.
VARIANT 447 447 A -> T (in allele CYP8A1*5; results in a
significantly decreased enzyme activity;
dbSNP:rs146531327).
{ECO:0000269|PubMed:25623425}.
/FTId=VAR_073186.
VARIANT 500 500 P -> S (in dbSNP:rs5584).
/FTId=VAR_014637.
TURN 38 40 {ECO:0000244|PDB:3B6H}.
HELIX 43 48 {ECO:0000244|PDB:3B6H}.
HELIX 50 61 {ECO:0000244|PDB:3B6H}.
STRAND 63 69 {ECO:0000244|PDB:3B6H}.
STRAND 72 77 {ECO:0000244|PDB:3B6H}.
HELIX 80 82 {ECO:0000244|PDB:3B6H}.
HELIX 83 87 {ECO:0000244|PDB:3B6H}.
TURN 91 93 {ECO:0000244|PDB:3B6H}.
STRAND 94 96 {ECO:0000244|PDB:2IAG}.
HELIX 98 106 {ECO:0000244|PDB:3B6H}.
HELIX 117 125 {ECO:0000244|PDB:3B6H}.
HELIX 130 155 {ECO:0000244|PDB:3B6H}.
STRAND 160 163 {ECO:0000244|PDB:3B6H}.
HELIX 164 181 {ECO:0000244|PDB:3B6H}.
HELIX 190 219 {ECO:0000244|PDB:3B6H}.
HELIX 224 240 {ECO:0000244|PDB:3B6H}.
HELIX 243 246 {ECO:0000244|PDB:3B6H}.
HELIX 254 265 {ECO:0000244|PDB:3B6H}.
HELIX 270 285 {ECO:0000244|PDB:3B6H}.
HELIX 288 300 {ECO:0000244|PDB:3B6H}.
HELIX 303 318 {ECO:0000244|PDB:3B6H}.
HELIX 333 336 {ECO:0000244|PDB:3B6H}.
HELIX 339 352 {ECO:0000244|PDB:3B6H}.
STRAND 357 361 {ECO:0000244|PDB:3B6H}.
STRAND 365 368 {ECO:0000244|PDB:3B6H}.
STRAND 374 377 {ECO:0000244|PDB:3B6H}.
STRAND 382 385 {ECO:0000244|PDB:3B6H}.
HELIX 388 392 {ECO:0000244|PDB:3B6H}.
TURN 395 397 {ECO:0000244|PDB:3B6H}.
STRAND 398 400 {ECO:0000244|PDB:3B6H}.
TURN 406 409 {ECO:0000244|PDB:3B6H}.
STRAND 414 416 {ECO:0000244|PDB:3B6H}.
HELIX 444 460 {ECO:0000244|PDB:3B6H}.
STRAND 462 468 {ECO:0000244|PDB:3B6H}.
HELIX 478 480 {ECO:0000244|PDB:3B6H}.
STRAND 482 485 {ECO:0000244|PDB:3B6H}.
STRAND 488 490 {ECO:0000244|PDB:3B6H}.
STRAND 493 498 {ECO:0000244|PDB:3B6H}.
SEQUENCE 500 AA; 57104 MW; 39595442BFC0B625 CRC64;
MAWAALLGLL AALLLLLLLS RRRTRRPGEP PLDLGSIPWL GYALDFGKDA ASFLTRMKEK
HGDIFTILVG GRYVTVLLDP HSYDAVVWEP RTRLDFHAYA IFLMERIFDV QLPHYSPSDE
KARMKLTLLH RELQALTEAM YTNLHAVLLG DATEAGSGWH EMGLLDFSYS FLLRAGYLTL
YGIEALPRTH ESQAQDRVHS ADVFHTFRQL DRLLPKLARG SLSVGDKDHM CSVKSRLWKL
LSPARLARRA HRSKWLESYL LHLEEMGVSE EMQARALVLQ LWATQGNMGP AAFWLLLFLL
KNPEALAAVR GELESILWQA EQPVSQTTTL PQKVLDSTPV LDSVLSESLR LTAAPFITRE
VVVDLAMPMA DGREFNLRRG DRLLLFPFLS PQRDPEIYTD PEVFKYNRFL NPDGSEKKDF
YKDGKRLKNY NMPWGAGHNH CLGRSYAVNS IKQFVFLVLV HLDLELINAD VEIPEFDLSR
YGFGLMQPEH DVPVRYRIRP


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E0699h ELISA kit COX2,COX-2,Cyclooxygenase-2,Homo sapiens,Human,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
E0122h ELISA kit COX1,COX-1,Cyclooxygenase-1,Homo sapiens,Human,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
U0699h CLIA COX2,COX-2,Cyclooxygenase-2,Homo sapiens,Human,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
U0699Rb CLIA COX2,COX-2,COX-2,Cyclooxygenase-2,Oryctolagus cuniculus,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2,Rabbit 96T
E0699h ELISA COX2,COX-2,Cyclooxygenase-2,Homo sapiens,Human,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
E0122h ELISA COX1,COX-1,Cyclooxygenase-1,Homo sapiens,Human,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0699Rb ELISA COX2,COX-2,COX-2,Cyclooxygenase-2,Oryctolagus cuniculus,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2,Rabbit 96T
E0122Rb ELISA kit COX1,COX-1,Cyclooxygenase-1,Oryctolagus cuniculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1,Rabbit 96T
E0122Rb ELISA COX1,COX-1,Cyclooxygenase-1,Oryctolagus cuniculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1,Rabbit 96T
U0122h CLIA COX1,COX-1,Cyclooxygenase-1,Homo sapiens,Human,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0122m ELISA Cox1,COX-1,Cox-1,Cyclooxygenase-1,Mouse,Mus musculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1 96T


 

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