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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2)

 PGH2_RAT                Reviewed;         604 AA.
P35355; Q64379; Q925V4;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 168.
RecName: Full=Prostaglandin G/H synthase 2;
EC=1.14.99.1;
AltName: Full=Cyclooxygenase-2;
Short=COX-2;
AltName: Full=PHS II;
AltName: Full=Prostaglandin H2 synthase 2;
Short=PGH synthase 2;
Short=PGHS-2;
AltName: Full=Prostaglandin-endoperoxide synthase 2;
Flags: Precursor;
Name=Ptgs2; Synonyms=Cox-2, Cox2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7916614; DOI=10.1006/bbrc.1993.2506;
Kennedy B.P., Chan C.C., Culp S.A., Cromlish W.A.;
"Cloning and expression of rat prostaglandin endoperoxide synthase
(cyclooxygenase)-2 cDNA.";
Biochem. Biophys. Res. Commun. 197:494-500(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8352945; DOI=10.1016/0896-6273(93)90192-T;
Yamagata K., Andreasson K.I., Kaufmann W.E., Barnes C.A., Worley P.F.;
"Expression of a mitogen-inducible cyclooxygenase in brain neurons:
regulation by synaptic activity and glucocorticoids.";
Neuron 11:371-386(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Intestine;
PubMed=8203528;
Dubois R.N., Tsujii M., Bishop P., Awad J.A., Makita K., Lanahan A.;
"Cloning and characterization of a growth factor-inducible
cyclooxygenase gene from rat intestinal epithelial cells.";
Am. J. Physiol. 266:G822-G827(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer 344;
PubMed=8274023; DOI=10.1006/abbi.1993.1601;
Feng L., Sun W., Xia Y., Tang W.W., Chanmugam P., Soyoola E.,
Wilson C.B., Hwang D.;
"Cloning two isoforms of rat cyclooxygenase: differential regulation
of their expression.";
Arch. Biochem. Biophys. 307:361-368(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10816563; DOI=10.1074/jbc.M001611200;
Xu K., Robida A.M., Murphy T.J.;
"Immediate-early MEK-1-dependent stabilization of rat smooth muscle
cell cyclooxygenase-2 mRNA by Galpha(q)-coupled receptor signaling.";
J. Biol. Chem. 275:23012-23019(2000).
[6]
PROTEIN SEQUENCE OF 18-43.
PubMed=1556140;
Sirois J., Richards J.S.;
"Purification and characterization of a novel, distinct isoform of
prostaglandin endoperoxide synthase induced by human chorionic
gonadotropin in granulosa cells of rat preovulatory follicles.";
J. Biol. Chem. 267:6382-6388(1992).
[7]
REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
Smith W.L., DeWitt D.L., Garavito R.M.;
"Cyclooxygenases: structural, cellular, and molecular biology.";
Annu. Rev. Biochem. 69:145-182(2000).
[8]
REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
COLORECTAL CANCER.
PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
Sostres C., Gargallo C.J., Lanas A.;
"Aspirin, cyclooxygenase inhibition and colorectal cancer.";
World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
-!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
committed step in prostanoid synthesis. Constitutively expressed
in some tissues in physiological conditions, such as the
endothelium, kidney and brain, and in pathological conditions,
such as in cancer. PTGS2 is responsible for production of
inflammatory prostaglandins. Up-regulation of PTGS2 is also
associated with increased cell adhesion, phenotypic changes,
resistance to apoptosis and tumor angiogenesis. In cancer cells,
PTGS2 is a key step in the production of prostaglandin E2 (PGE2),
which plays important roles in modulating motility, proliferation
and resistance to apoptosis.
-!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
H(2) + A + H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000250};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
protein. Endoplasmic reticulum membrane; Peripheral membrane
protein.
-!- TISSUE SPECIFICITY: Expressed throughout the forebrain in discrete
populations of neurons and is enriched in the cortex and
hippocampus.
-!- INDUCTION: By cytokines and mitogens.
-!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-
nitrosylation may take place on different Cys residues in addition
to Cys-526 (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
is a 2 step reaction: a cyclooxygenase (COX) reaction which
converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
cyclooxygenase reaction occurs in a hydrophobic channel in the
core of the enzyme. The peroxidase reaction occurs at a heme-
containing active site located near the protein surface. The
nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
corresponds to the cyclooxygenase active site.
-!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
mediated by 2 different isozymes: the constitutive PTGS1 and the
inducible PTGS2. PGHS1 is expressed constitutively and generally
produces prostanoids acutely in response to hormonal stimuli to
fine-tune physiological processes requiring instantaneous,
continuous regulation (e.g. hemostasis). PGHS2 is inducible and
typically produces prostanoids that mediate responses to
physiological stresses such as infection and inflammation.
-!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen.
Aspirin is able to produce an irreversible inactivation of the
enzyme through a serine acetylation. Inhibition of the PGHSs with
NSAIDs acutely reduces inflammation, pain, and fever, and long-
term use of these drugs reduces fatal thrombotic events, as well
as the development of colon cancer and Alzheimer's disease. PTGS2
is the principal isozyme responsible for production of
inflammatory prostaglandins. New generation PTGSs inhibitors
strive to be selective for PTGS2, to avoid side effects such as
gastrointestinal complications and ulceration.
-!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
{ECO:0000305}.
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EMBL; L25925; AAA16477.1; -; mRNA.
EMBL; U04300; AAA20246.1; -; mRNA.
EMBL; U03389; AAA03466.1; -; mRNA.
EMBL; S67722; AAB29401.1; -; mRNA.
EMBL; AF233596; AAF36986.1; -; mRNA.
PIR; JC2030; JC2030.
RefSeq; NP_058928.3; NM_017232.3.
UniGene; Rn.217585; -.
UniGene; Rn.44369; -.
ProteinModelPortal; P35355; -.
SMR; P35355; -.
BioGrid; 248163; 5.
CORUM; P35355; -.
IntAct; P35355; 1.
STRING; 10116.ENSRNOP00000003567; -.
BindingDB; P35355; -.
ChEMBL; CHEMBL2977; -.
PeroxiBase; 3975; RnoPGHS02-A.
iPTMnet; P35355; -.
PhosphoSitePlus; P35355; -.
PaxDb; P35355; -.
PRIDE; P35355; -.
Ensembl; ENSRNOT00000003567; ENSRNOP00000003567; ENSRNOG00000002525.
GeneID; 29527; -.
KEGG; rno:29527; -.
UCSC; RGD:620349; rat.
CTD; 5743; -.
RGD; 620349; Ptgs2.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
HOVERGEN; HBG000366; -.
InParanoid; P35355; -.
KO; K11987; -.
OMA; CNNVKGC; -.
OrthoDB; EOG091G03CD; -.
PhylomeDB; P35355; -.
TreeFam; TF329675; -.
BRENDA; 1.14.99.1; 5301.
Reactome; R-RNO-197264; Nicotinamide salvaging.
Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-RNO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
UniPathway; UPA00662; -.
PRO; PR:P35355; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000002525; -.
Genevisible; P35355; RN.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; ISO:RGD.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:RGD.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0001525; P:angiogenesis; IMP:RGD.
GO; GO:0030282; P:bone mineralization; IMP:MGI.
GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
GO; GO:0071318; P:cellular response to ATP; IEP:RGD.
GO; GO:0071498; P:cellular response to fluid shear stress; ISO:RGD.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071471; P:cellular response to non-ionic osmotic stress; ISO:RGD.
GO; GO:0034644; P:cellular response to UV; IEP:RGD.
GO; GO:0019371; P:cyclooxygenase pathway; ISS:UniProtKB.
GO; GO:0046697; P:decidualization; IMP:RGD.
GO; GO:0007566; P:embryo implantation; IMP:RGD.
GO; GO:0042633; P:hair cycle; IEP:RGD.
GO; GO:0006954; P:inflammatory response; IMP:RGD.
GO; GO:0007612; P:learning; IMP:RGD.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IMP:RGD.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IMP:RGD.
GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:RGD.
GO; GO:0045786; P:negative regulation of cell cycle; IGI:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; ISO:RGD.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IMP:RGD.
GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IMP:RGD.
GO; GO:0030728; P:ovulation; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISO:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IMP:BHF-UCL.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; IMP:BHF-UCL.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:RGD.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:RGD.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IMP:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:RGD.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISO:RGD.
GO; GO:1990776; P:response to angiotensin; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IMP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0009750; P:response to fructose; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR029576; COX-2.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
PANTHER; PTHR11903:SF8; PTHR11903:SF8; 1.
Pfam; PF03098; An_peroxidase; 2.
Pfam; PF00008; EGF; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
Complete proteome; Dioxygenase; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase;
Peroxidase; Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; S-nitrosylation; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:1556140}.
CHAIN 18 604 Prostaglandin G/H synthase 2.
/FTId=PRO_0000023879.
DOMAIN 18 55 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
ACT_SITE 371 371 For cyclooxygenase activity.
{ECO:0000250}.
METAL 374 374 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
BINDING 106 106 Substrate. {ECO:0000250}.
BINDING 341 341 Substrate. {ECO:0000250}.
BINDING 371 371 Substrate. {ECO:0000250}.
SITE 516 516 Aspirin-acetylated serine. {ECO:0000250}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 21 32 {ECO:0000250}.
DISULFID 22 145 {ECO:0000250}.
DISULFID 26 42 {ECO:0000250}.
DISULFID 44 54 {ECO:0000250}.
DISULFID 555 561 {ECO:0000250}.
CONFLICT 11 13 ALA -> CPG (in Ref. 4 and 5).
{ECO:0000305}.
CONFLICT 58 58 E -> R (in Ref. 4 and 5). {ECO:0000305}.
CONFLICT 66 66 L -> P (in Ref. 4 and 5). {ECO:0000305}.
CONFLICT 96 98 NSI -> IQS (in Ref. 4 and 5).
{ECO:0000305}.
CONFLICT 339 339 S -> R (in Ref. 4 and 5). {ECO:0000305}.
CONFLICT 344 344 K -> Q (in Ref. 4 and 5). {ECO:0000305}.
CONFLICT 350 350 E -> D (in Ref. 4 and 5). {ECO:0000305}.
CONFLICT 368 368 N -> K (in Ref. 4 and 5). {ECO:0000305}.
CONFLICT 573 573 P -> A (in Ref. 4 and 5). {ECO:0000305}.
SEQUENCE 604 AA; 69164 MW; 98E418825D98FF0C CRC64;
MLFRAVLLCA ALALSHAANP CCSNPCQNRG ECMSIGFDQY KCDCTRTGFY GENCTTPEFL
TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRNSIMR YVLTSRSHLI DSPPTYNVHY
GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGNKELPDS KEVLEKVLLR REFIPDPQGT
NMMFAFFAQH FTHQFFKTDQ KRGPGFTRGL GHGVDLNHVY GETLDRQHKL RLFQDGKLKY
QVIGGEVYPP TVKDTQVDMI YPPHVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
ILKQEHPEWD DERLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ
NRIASEFNTL YHWHPLLPDT FNIEDQEYTF KQFLYNNSIL LEHGLAHFVE SFTRQIAGRV
AGGRNVPIAV QAVAKASIDQ SREMKYQSLN EYRKRFSLKP YTSFEELTGE KEMAAELKAL
YHDIDAMELY PALLVEKPRP DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV
GFRIINTASI QSLICNNVKG CPFASFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR
STEL


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E0122b ELISA kit Bos taurus,Bovine,COX1,COX-1,COX-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0122m ELISA kit 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
U0122b CLIA Bos taurus,Bovine,COX1,COX-1,COX-1,Cyclooxygenase-1,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
E0699b ELISA kit Bos taurus,Bovine,COX2,COX-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
U0122r CLIA Cox1,COX-1,Cox-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1,Rat,Rattus norvegicus 96T
E0699r ELISA Cox2,COX-2,Cox-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,Ptgs2,Rat,Rattus norvegicus 96T
E0699r ELISA kit Cox2,COX-2,Cox-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,Ptgs2,Rat,Rattus norvegicus 96T


 

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