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Pentafunctional AROM polypeptide [Includes: Shikimate dehydrogenase (EC 1.1.1.25); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS)]

 A0A1X6N1M2_9APHY        Unreviewed;      1640 AA.
A0A1X6N1M2;
05-JUL-2017, integrated into UniProtKB/TrEMBL.
05-JUL-2017, sequence version 1.
12-SEP-2018, entry version 13.
RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=SK {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143};
AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=POSPLADRAFT_1142536 {ECO:0000313|EMBL:OSX62353.1};
Postia placenta MAD-698-R-SB12.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Dacryobolaceae; Postia.
NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX62353.1};
[1] {ECO:0000313|EMBL:OSX62353.1}
NUCLEOTIDE SEQUENCE.
STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX62353.1};
DOE Joint Genome Institute;
Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D.,
Hibbett D., Schmoll M., Kubicek C.P., Martinez A.T., Yadav J.,
Master E., Magnuson J.K., James T., Yaver D., Berka R., Labutti K.,
Lipzen A., Aerts A., Barry K., Henrissat B., Blanchette R.,
Grigoriev I., Cullen D.;
"Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712173}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712185}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712180}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858971}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712175}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712177}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629576}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629599}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-
dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712181}.
-!- SIMILARITY: In the N-terminal section; belongs to the
dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar
phosphate cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
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EMBL; KZ110597; OSX62353.1; -; Genomic_DNA.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00502; DHQase_I; 1.
CDD; cd01556; EPSP_synthase; 1.
CDD; cd00464; SK; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.65.10.10; -; 2.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00222; Shikimate_DH_AroE; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008289; Pentafunct_AroM.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR010110; Shikimate_DH_AroM-type.
InterPro; IPR022893; Shikimate_DH_fam.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF01488; Shikimate_DH; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PROSITE; PS01128; SHIKIMATE_KINASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629772};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727050};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629584};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
DOMAIN 74 359 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 411 852 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1339 1420 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1455 1509 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 80 83 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 111 113 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 136 137 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 176 179 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 890 897 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 385 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 191 194 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 265 269 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1334 1640 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 261 261 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 276 276 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 840 840 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1223 1223 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1251 1251 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 191 191 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 272 272 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 288 288 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 116 116 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 127 127 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 143 143 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 149 149 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 158 158 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 159 159 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 187 187 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 251 251 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 272 272 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 288 288 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 357 357 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1640 AA; 176678 MW; AE758E5E41A264C7 CRC64;
MSSADIQKVS ILGKESIHCG FHLIPYIVNT VLTALPSSTY VIVTDINIAS LHLVAFQTAF
KKHTLSSKAR FLNYVVPPGE TSKSREGKAE IEDYLLLNAS TRDTVILALG GGVIGDLVGF
VAATFMRGVR FVQIPTTLLA MVDSSVGGKT AIDTPHGKNL IGAFWQPEYI FIDAAFLETL
PAREFSNGMA EVVKTAAIWN EDEFSALESR SAELFAAIQT PSKDNSGRMV ATRSAAQQLL
LSVIVGSISV KAHIVTVDER ETGLRNLVNF GHTIGHAIEA VLTPSMLHGE CVSVGMILEA
EVARSLGVLG QVAVGRLTRC LKAYNLPVSL SDSRIVRLPA ARGLGVERLL DIMKIDKKNS
GAQKKIVILS RIGATYEQKA TVVADSVIAK TLSEAVVVVP GVPSKSPVRM ATPGSKSISN
RALLLAALGK GTCRLKNLLH SDDTQVMMNA LQELKGARFS WEDGGETLVV HGGEGSLSVP
PAGKEVYLGN AGTAARFLTT VCTLVQSATP GERTVITGNA RMKQRPIGPL VDALRTNGSD
IEYKESQGCL PLSVAPAGLK GARIQLAASV SSQYVSSILL CAPYAREPVT LELTGGQVIS
QPYIDMTIAI MKTFGIDVVR EVDQATGAPL DVYHIPAGVY TNPPLYNIES DASSATYPLA
VAAITGTTCT IMNIGSSSLQ GDARFAKEVL EPMGCKVVQT ETETTVTGPP IGQLKALGTV
DMEPMTDAFL TASVLAAVAT GAPSKGRELA DGSRLTTTRI IGIANQRVKE CNRIQAMIDQ
LAKFGVETKE LEDGLEVYGK PISELKEGAS IHCYDDHRVA MAFSVLASAV RGTIIEEKRC
VEKTWPNWWD DLENKIGLGV EGVELPVHVS STSTSRPVDA DVSASVVIIG MRGSGKTFIG
QLAASILDWQ FLDADAVFEE KHQTGVRDFV HQHGWPTFRD AETVVLQELL AEKPTGHIIS
LGGGIVETPA ARSLLQTYAE RGPVVHIKRD IDEIVSYLGE ETARPAYGEP ILDVFKRRQP
WFAECCSYVF VNNTGGLESA EESVAGGTAV PLQSTTHPSS TSLRNETERF FNHVTGSKPN
LALTAMDDKR TYFLSLTYPD VKQALSHIED LTTGVDAIEL RVDLLRSYDD HVKLEPYIPS
VEYVTDQITS LRRRTTLPIV FTVRTVSQGG RFPDDAEKEA FELFHTALRL AVEYIDVEIS
WTEGQIKNLA AHKGHSQIIA SWHDWSGKMQ WDGKGVEAKY RLAASMGDIV KIVGKANDLN
DNLALHRFAQ RMRLLPDSKP MIGINMGIEG QLSRILNSTL SPVSHPLLPT KAAPGQLSFA
QIQSALHLIG QSPSQRFYLF GNPIAHSMSP TLHNTAFEIL GLPHTYDLLQ TDSVGEEIRA
ALASPEFGGA SVTIPFKLDI IPLLDLLSPE AEAIGAVNTI VPRRGTDGSL MLYGDNTDWL
GIMQCIRSAW PNAALKPDTA LVIGAGGTSR AAIYALGRLG VNAVYIYNRT RSSVQALVEA
FPGVKVEAID TLGRWPQGGR SPSIVISTVP ASATTADLKV KNALYLPSSI FAAGSEGVVV
DMAYKPAETP LLVLASKVAK NWKRVRGVEV LLEQGYRQFN LWTGRQCPKR LAALRLGLLI
VDHPCFVAGT LLQADRSQST


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U0167m CLIA 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
E0167m ELISA 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
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
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
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
E0167r ELISA kit 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
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


 

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