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Tricyclene synthase, chloroplastic (EC 4.2.3.105) ((E)-beta-ocimene synthase) (EC 4.2.3.106) ((E,E)-alpha-farnesene synthase) (EC 4.2.3.46) (Terpenoid synthase 3) (AtTPS03)

 TPS03_ARATH             Reviewed;         565 AA.
A4FVP2; O23517; Q84NE5; Q8GWA8; Q8LE37; Q9FVI5;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 1.
22-NOV-2017, entry version 82.
RecName: Full=Tricyclene synthase, chloroplastic;
EC=4.2.3.105;
AltName: Full=(E)-beta-ocimene synthase;
EC=4.2.3.106;
AltName: Full=(E,E)-alpha-farnesene synthase;
EC=4.2.3.46;
AltName: Full=Terpenoid synthase 3;
Short=AtTPS03;
Flags: Precursor;
Name=TPS03; OrderedLocusNames=At4g16740; ORFNames=dl4395w, FCAALL.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C.,
Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-565 (ISOFORM 1), FUNCTION, AND
INDUCTION.
STRAIN=cv. C24;
PubMed=12624761; DOI=10.1007/s00425-002-0924-0;
Faeldt J., Arimura G., Gershenzon J., Takabayashi J., Bohlmann J.;
"Functional identification of AtTPS03 as (E)-beta-ocimene synthase: a
monoterpene synthase catalyzing jasmonate- and wound-induced volatile
formation in Arabidopsis thaliana.";
Planta 216:745-751(2003).
[8]
NUCLEOTIDE SEQUENCE OF 163-292 (ISOFORMS 1/2).
Bohlmann J.;
"cDNA fragment of a monoterpene synthase AtTPS03 from Arabidopisis
thaliana.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[9]
INDUCTION BY HERBIVORY.
PubMed=11710601; DOI=10.1023/A:1012213116515;
Van Poecke R.M., Posthumus M.A., Dicke M.;
"Herbivore-induced volatile production by Arabidopsis thaliana leads
to attraction of the parasitoid Cotesia rubecula: chemical,
behavioral, and gene-expression analysis.";
J. Chem. Ecol. 27:1911-1928(2001).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
Aubourg S., Lecharny A., Bohlmann J.;
"Genomic analysis of the terpenoid synthase (AtTPS) gene family of
Arabidopsis thaliana.";
Mol. Genet. Genomics 267:730-745(2002).
[11]
TISSUE SPECIFICITY.
PubMed=12566586; DOI=10.1105/tpc.007989;
Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E.,
Gershenzon J.;
"Biosynthesis and emission of terpenoid volatiles from Arabidopsis
flowers.";
Plant Cell 15:481-494(2003).
[12]
GENE FAMILY.
PubMed=12777052; DOI=10.1023/A:1023005504702;
Lange B.M., Ghassemian M.;
"Genome organization in Arabidopsis thaliana: a survey for genes
involved in isoprenoid and chlorophyll metabolism.";
Plant Mol. Biol. 51:925-948(2003).
[13]
TISSUE SPECIFICITY.
PubMed=16297850; DOI=10.1016/j.abb.2005.09.019;
Ro D.-K., Ehlting J., Keeling C.I., Lin R., Mattheus N., Bohlmann J.;
"Microarray expression profiling and functional characterization of
AtTPS genes: duplicated Arabidopsis thaliana sesquiterpene synthase
genes At4g13280 and At4g13300 encode root-specific and wound-inducible
(Z)-gamma-bisabolene synthases.";
Arch. Biochem. Biophys. 448:104-116(2006).
[14]
INDUCTION BY WOUNDING.
PubMed=17905899; DOI=10.1105/tpc.106.049981;
Catala R., Ouyang J., Abreu I.A., Hu Y., Seo H., Zhang X., Chua N.H.;
"The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and
drought responses.";
Plant Cell 19:2952-2966(2007).
[15]
FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=20463089; DOI=10.1104/pp.110.154864;
Huang M., Abel C., Sohrabi R., Petri J., Haupt I., Cosimano J.,
Gershenzon J., Tholl D.;
"Variation of herbivore-induced volatile terpenes among Arabidopsis
ecotypes depends on allelic differences and subcellular targeting of
two terpene synthases, TPS02 and TPS03.";
Plant Physiol. 153:1293-1310(2010).
-!- FUNCTION: Predominantly involved in sesquiterpenes (C15)
biosynthesis. Using FPP as substrate, the major product is (E,E)-
alpha-farnesene with minor amounts of (Z,E)-alpha-farnesene and
(E,E)-beta-farnesene. Using GPP as substrate, could also be able
in vitro to synthesize monoterpene (C10) with (E)-beta-ocimene as
the major product and with (Z)-beta-ocimene and myrcene as minor
products. {ECO:0000269|PubMed:12624761,
ECO:0000269|PubMed:20463089}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-
farnesene + diphosphate.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate = tricyclene +
diphosphate.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate = (E)-beta-ocimene +
diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
-!- PATHWAY: Secondary metabolite biosynthesis; terpenoid
biosynthesis.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20463089}.
Plastid, chloroplast stroma {ECO:0000269|PubMed:20463089}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=A4FVP2-1; Sequence=Displayed;
Name=2;
IsoId=A4FVP2-2; Sequence=VSP_035151, VSP_035152;
Note=Derived from EST data. No experimental confirmation
available.;
Name=3;
IsoId=A4FVP2-3; Sequence=VSP_044001, VSP_044002;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in flowers but also in
leaves, roots, stems and siliques. {ECO:0000269|PubMed:12566586,
ECO:0000269|PubMed:16297850}.
-!- INDUCTION: By coronalon, jasmonic acid and wounding, but not by
salicylic acid, cimene and limonene. Also induced in response to
the caterpillar P.xylostella or P.rapae feeding.
{ECO:0000269|PubMed:11710601, ECO:0000269|PubMed:12624761,
ECO:0000269|PubMed:17905899, ECO:0000269|PubMed:20463089}.
-!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important
for the catalytic activity, presumably through binding to Mg(2+).
-!- DISRUPTION PHENOTYPE: Reduction of TMTT, MeSA and (E,E)-alpha-
farnesene emmission. No formation of (E)-beta-ocimene detected.
{ECO:0000269|PubMed:20463089}.
-!- SIMILARITY: Belongs to the terpene synthase family. Tpsb
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB10449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB78716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; Z97341; CAB10449.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161544; CAB78716.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE83793.1; -; Genomic_DNA.
EMBL; CP002687; AEE83794.1; -; Genomic_DNA.
EMBL; AK118969; BAC43546.1; -; mRNA.
EMBL; BT030340; ABO38753.1; -; mRNA.
EMBL; AY085646; AAM62867.1; -; mRNA.
EMBL; AY151086; AAN65379.1; -; mRNA.
EMBL; AF180366; AAG09423.1; -; mRNA.
PIR; G71434; G71434.
RefSeq; NP_001031651.1; NM_001036574.1. [A4FVP2-2]
RefSeq; NP_567511.3; NM_117775.4. [A4FVP2-1]
UniGene; At.44857; -.
ProteinModelPortal; A4FVP2; -.
SMR; A4FVP2; -.
STRING; 3702.AT4G16740.1; -.
PaxDb; A4FVP2; -.
EnsemblPlants; AT4G16740.1; AT4G16740.1; AT4G16740. [A4FVP2-1]
EnsemblPlants; AT4G16740.2; AT4G16740.2; AT4G16740. [A4FVP2-2]
GeneID; 827377; -.
Gramene; AT4G16740.1; AT4G16740.1; AT4G16740.
Gramene; AT4G16740.2; AT4G16740.2; AT4G16740.
KEGG; ath:AT4G16740; -.
Araport; AT4G16740; -.
TAIR; locus:2129101; AT4G16740.
eggNOG; ENOG410II1F; Eukaryota.
eggNOG; ENOG410YF98; LUCA.
HOGENOM; HOG000232971; -.
InParanoid; A4FVP2; -.
KO; K19968; -.
OMA; TIVEKWD; -.
OrthoDB; EOG093607JQ; -.
PhylomeDB; A4FVP2; -.
BioCyc; ARA:AT4G16740-MONOMER; -.
BioCyc; MetaCyc:AT4G16740-MONOMER; -.
BRENDA; 4.2.3.106; 399.
BRENDA; 4.2.3.46; 399.
BRENDA; 4.2.3.B40; 399.
UniPathway; UPA00213; -.
PRO; PR:A4FVP2; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; A4FVP2; baseline and differential.
Genevisible; A4FVP2; AT.
GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:UniProtKB.
GO; GO:0052578; F:alpha-farnesene synthase activity; IMP:TAIR.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0050551; F:myrcene synthase activity; IDA:TAIR.
GO; GO:0010333; F:terpene synthase activity; ISS:UniProtKB.
GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
GO; GO:0009625; P:response to insect; IEP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IMP:TAIR.
Gene3D; 1.10.600.10; -; 1.
Gene3D; 1.50.10.130; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR034741; Terpene_cyclase_like_1_C.
InterPro; IPR001906; Terpene_synth_N.
InterPro; IPR036965; Terpene_synth_N_sf.
InterPro; IPR005630; Terpene_synthase_metal-bd.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF01397; Terpene_synth; 1.
Pfam; PF03936; Terpene_synth_C; 1.
SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF48576; SSF48576; 1.
2: Evidence at transcript level;
Alternative splicing; Chloroplast; Complete proteome; Cytoplasm;
Lyase; Magnesium; Manganese; Metal-binding; Plastid;
Reference proteome; Transit peptide.
TRANSIT 1 25 Chloroplast. {ECO:0000255}.
CHAIN 26 565 Tricyclene synthase, chloroplastic.
/FTId=PRO_0000348422.
MOTIF 320 324 DDXXD motif.
METAL 320 320 Magnesium or manganese 1. {ECO:0000250}.
METAL 320 320 Magnesium or manganese 2. {ECO:0000250}.
METAL 324 324 Magnesium or manganese 1. {ECO:0000250}.
METAL 324 324 Magnesium or manganese 2. {ECO:0000250}.
METAL 461 461 Magnesium or manganese 3. {ECO:0000250}.
METAL 465 465 Magnesium or manganese 3. {ECO:0000250}.
METAL 469 469 Magnesium or manganese 3. {ECO:0000250}.
VAR_SEQ 144 144 D -> G (in isoform 3).
{ECO:0000303|PubMed:11910074,
ECO:0000303|Ref.6}.
/FTId=VSP_044001.
VAR_SEQ 145 565 Missing (in isoform 3).
{ECO:0000303|PubMed:11910074,
ECO:0000303|Ref.6}.
/FTId=VSP_044002.
VAR_SEQ 388 396 WADMCTTFL -> VRILIILSM (in isoform 2).
{ECO:0000305}.
/FTId=VSP_035151.
VAR_SEQ 397 565 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_035152.
CONFLICT 27 27 R -> L (in Ref. 6; AAM62867).
{ECO:0000305}.
CONFLICT 69 69 N -> D (in Ref. 4; BAC43546).
{ECO:0000305}.
CONFLICT 182 182 S -> T (in Ref. 8; AAG09423).
{ECO:0000305}.
CONFLICT 289 289 G -> S (in Ref. 8; AAG09423).
{ECO:0000305}.
SEQUENCE 565 AA; 65753 MW; 126B4800002A2ECD CRC64;
MPKRQAQRRF TRKTDSKTPS QPLVSRRSAN YQPSLWQHEY LLSLGNTYVK EDNVERVTLL
KQEVSKMLNE TEGLLEQLEL IDTLQRLGVS YHFEQEIKKT LTNVHVKNVR AHKNRIDRNR
WGDLYATALE FRLLRQHGFS IAQDVFDGNI GVDLDDKDIK GILSLYEASY LSTRIDTKLK
ESIYYTTKRL RKFVEVNKNE TKSYTLRRMV IHALEMPYHR RVGRLEARWY IEVYGERHDM
NPILLELAKL DFNFVQAIHQ DELKSLSSWW SKTGLTKHLD FVRDRITEGY FSSVGVMYEP
EFAYHRQMLT KVFMLITTID DIYDIYGTLE ELQLFTTIVE KWDVNRLEEL PNYMKLCFLC
LVNEINQIGY FVLRDKGFNV IPYLKESWAD MCTTFLKEAK WYKSGYKPNF EEYMQNGWIS
SSVPTILLHL FCLLSDQTLD ILGSYNHSVV RSSATILRLA NDLATSSEEL ARGDTMKSVQ
CHMHETGASE AESRAYIQGI IGVAWDDLNM EKKSCRLHQG FLEAAANLGR VAQCVYQYGD
GHGCPDKAKT VNHVRSLLVH PLPLN


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U0167r CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167b ELISA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167b ELISA kit Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167r ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
E0167m ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167p ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
E0167p ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
U0167p CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 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
U0122Rb CLIA 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
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
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


 

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