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Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1)

 PGH1_SHEEP              Reviewed;         600 AA.
P05979;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
04-FEB-2015, sequence version 3.
25-OCT-2017, entry version 155.
RecName: Full=Prostaglandin G/H synthase 1;
EC=1.14.99.1;
AltName: Full=Cyclooxygenase-1;
Short=COX-1;
AltName: Full=Prostaglandin H2 synthase 1;
Short=PGH synthase 1;
Short=PGHS-1;
Short=PHS 1;
AltName: Full=Prostaglandin-endoperoxide synthase 1;
Flags: Precursor;
Name=PTGS1; Synonyms=COX1;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
GLY-164.
TISSUE=Seminal vesicle;
PubMed=3125548; DOI=10.1073/pnas.85.5.1412;
Dewitt D.L., Smith W.L.;
"Primary structure of prostaglandin G/H synthase from sheep vesicular
gland determined from the complementary DNA sequence.";
Proc. Natl. Acad. Sci. U.S.A. 85:1412-1416(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3129310; DOI=10.1016/0014-5793(88)80847-0;
Yokoyama C., Takai T., Tanabe T.;
"Primary structure of sheep prostaglandin endoperoxide synthase
deduced from cDNA sequence.";
FEBS Lett. 231:347-351(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-164.
PubMed=2831188;
Merlie J., Fagan D., Mudd J., Needleman P.;
"Isolation and characterization of the complementary DNA for sheep
seminal vesicle prostaglandin endoperoxide synthase
(cyclooxygenase).";
J. Biol. Chem. 263:3550-3553(1988).
[4]
PROTEIN SEQUENCE OF 523-544.
PubMed=6414516; DOI=10.1021/bi00289a010;
Roth G.J., Machuga E.T., Ozols J.;
"Isolation and covalent structure of the aspirin-modified, active-site
region of prostaglandin synthetase.";
Biochemistry 22:4672-4675(1983).
[5]
HEME-BINDING SITE.
PubMed=2108169;
Dewitt D.L., El-Harith E.A., Kraemer S.A., Andrews M.J., Yao E.F.,
Armstrong R.L., Smith W.L.;
"The aspirin and heme-binding sites of ovine and murine prostaglandin
endoperoxide synthases.";
J. Biol. Chem. 265:5192-5198(1990).
[6]
ACTIVE SITE TYR-385, AND MUTAGENESIS OF TYR-385.
PubMed=2122967;
Shimokawa T., Kulmacz R.J., Dewitt D.L., Smith W.L.;
"Tyrosine 385 of prostaglandin endoperoxide synthase is required for
cyclooxygenase catalysis.";
J. Biol. Chem. 265:20073-20076(1990).
[7]
GLYCOSYLATION AT ASN-68; ASN-144 AND ASN-410, AND LACK OF
GLYCOSYLATION AT ASN-104.
PubMed=8349699;
Otto J.C., Dewitt D.L., Smith W.L.;
"N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and
their orientations in the endoplasmic reticulum.";
J. Biol. Chem. 268:18234-18242(1993).
[8]
FUNCTION, AND INHIBITION BY NSAIDS.
PubMed=10438452; DOI=10.1074/jbc.274.33.22903;
Marnett L.J., Rowlinson S.W., Goodwin D.C., Kalgutkar A.S.,
Lanzo C.A.;
"Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of
catalysis and inhibition.";
J. Biol. Chem. 274:22903-22906(1999).
[9]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=8121489; DOI=10.1038/367243a0;
Picot D., Loll P.J., Garavito R.M.;
"The X-ray crystal structure of the membrane protein prostaglandin H2
synthase-1.";
Nature 367:243-249(1994).
[10]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
PubMed=7552725; DOI=10.1038/nsb0895-637;
Loll P.J., Picot D., Garavito R.M.;
"The structural basis of aspirin activity inferred from the crystal
structure of inactivated prostaglandin H2 synthase.";
Nat. Struct. Biol. 2:637-643(1995).
[11]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=8652509; DOI=10.1021/bi952776w;
Loll P.J., Picot D., Ekabo O., Garavito R.M.;
"Synthesis and use of iodinated antiinflammatory drug analogs as
crystallographic probes of the prostaglandin H2 synthase
cyclooxygenase active site.";
Biochemistry 35:7330-7340(1996).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=10988074; DOI=10.1126/science.289.5486.1933;
Malkowski M.G., Ginell S.L., Smith W.L., Garavito R.M.;
"The productive conformation of arachidonic acid bound to
prostaglandin synthase.";
Science 289:1933-1937(2000).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=11121413; DOI=10.1074/jbc.M009378200;
Thuresson E.D., Malkowski M.G., Lakkides K.M., Rieke C.J.,
Mulichak A.M., Ginell S.L., Garavito R.M., Smith W.L.;
"Mutational and X-ray crystallographic analysis of the interaction of
dihomo-gamma-linolenic acid with prostaglandin endoperoxide H
synthases.";
J. Biol. Chem. 276:10358-10365(2001).
[14]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
PubMed=11318639; DOI=10.1021/bi010045s;
Selinsky B.S., Gupta K., Sharkey C.T., Loll P.J.;
"Structural analysis of NSAID binding by prostaglandin H2 synthase:
time-dependent and time-independent inhibitors elicit identical enzyme
conformations.";
Biochemistry 40:5172-5180(2001).
-!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
committed step in prostanoid synthesis. Involved in the
constitutive production of prostanoids in particular in the
stomach and platelets. In gastric epithelial cells, it is a key
step in the generation of prostaglandins, such as prostaglandin E2
(PGE2), which plays an important role in cytoprotection. In
platelets, it is involved in the generation of thromboxane A2
(TXA2), which promotes platelet activation and aggregation,
vasoconstriction and proliferation of vascular smooth muscle
cells. {ECO:0000269|PubMed:10438452}.
-!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
H(2) + A + H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit.;
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Microsome membrane; Multi-pass membrane protein.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAA31576.1; Type=Frameshift; Positions=63, 92; Evidence={ECO:0000305};
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EMBL; J03599; AAA31576.1; ALT_FRAME; mRNA.
EMBL; Y00750; CAA68719.1; -; mRNA.
EMBL; M18243; AAA31511.1; -; mRNA.
PIR; A28960; A28960.
PIR; A29947; A29947.
PIR; S00561; S00561.
RefSeq; NP_001009476.1; NM_001009476.1.
UniGene; Oar.445; -.
PDB; 1CQE; X-ray; 3.10 A; A/B=21-600.
PDB; 1DIY; X-ray; 3.00 A; A=32-584.
PDB; 1DJJ; Model; -; A=25-600.
PDB; 1EBV; X-ray; 3.20 A; A=33-583.
PDB; 1EQG; X-ray; 2.61 A; A/B=21-600.
PDB; 1EQH; X-ray; 2.70 A; A/B=21-600.
PDB; 1FE2; X-ray; 3.00 A; A=25-600.
PDB; 1HT5; X-ray; 2.75 A; A/B=33-583.
PDB; 1HT8; X-ray; 2.69 A; A/B=33-583.
PDB; 1IGX; X-ray; 3.10 A; A=25-600.
PDB; 1IGZ; X-ray; 2.90 A; A=25-600.
PDB; 1PGE; X-ray; 3.50 A; A/B=25-600.
PDB; 1PGF; X-ray; 4.50 A; A/B=25-600.
PDB; 1PGG; X-ray; 4.50 A; A/B=25-600.
PDB; 1PRH; X-ray; 3.50 A; A/B=33-586.
PDB; 1PTH; X-ray; 3.40 A; A/B=25-600.
PDB; 1Q4G; X-ray; 2.00 A; A/B=32-584.
PDB; 1U67; X-ray; 3.10 A; A=1-600.
PDB; 2AYL; X-ray; 2.00 A; A/B=32-584.
PDB; 2OYE; X-ray; 2.85 A; P=1-600.
PDB; 2OYU; X-ray; 2.70 A; P=1-600.
PDB; 3KK6; X-ray; 2.75 A; A/B=32-584.
PDB; 3N8V; X-ray; 3.05 A; A/B=32-584.
PDB; 3N8W; X-ray; 2.75 A; A/B=32-584.
PDB; 3N8X; X-ray; 2.75 A; A/B=32-584.
PDB; 3N8Y; X-ray; 2.60 A; A/B=32-584.
PDB; 3N8Z; X-ray; 2.90 A; A/B=32-584.
PDB; 4O1Z; X-ray; 2.40 A; A/B=32-600.
PDB; 5U6X; X-ray; 2.93 A; A/B=1-600.
PDB; 5WBE; X-ray; 2.75 A; A/B=1-600.
PDBsum; 1CQE; -.
PDBsum; 1DIY; -.
PDBsum; 1DJJ; -.
PDBsum; 1EBV; -.
PDBsum; 1EQG; -.
PDBsum; 1EQH; -.
PDBsum; 1FE2; -.
PDBsum; 1HT5; -.
PDBsum; 1HT8; -.
PDBsum; 1IGX; -.
PDBsum; 1IGZ; -.
PDBsum; 1PGE; -.
PDBsum; 1PGF; -.
PDBsum; 1PGG; -.
PDBsum; 1PRH; -.
PDBsum; 1PTH; -.
PDBsum; 1Q4G; -.
PDBsum; 1U67; -.
PDBsum; 2AYL; -.
PDBsum; 2OYE; -.
PDBsum; 2OYU; -.
PDBsum; 3KK6; -.
PDBsum; 3N8V; -.
PDBsum; 3N8W; -.
PDBsum; 3N8X; -.
PDBsum; 3N8Y; -.
PDBsum; 3N8Z; -.
PDBsum; 4O1Z; -.
PDBsum; 5U6X; -.
PDBsum; 5WBE; -.
SMR; P05979; -.
BindingDB; P05979; -.
ChEMBL; CHEMBL2949; -.
PeroxiBase; 4121; OarPGHS01.
iPTMnet; P05979; -.
PRIDE; P05979; -.
GeneID; 443551; -.
KEGG; oas:443551; -.
CTD; 5742; -.
HOVERGEN; HBG000366; -.
KO; K00509; -.
BRENDA; 1.14.99.1; 2668.
SABIO-RK; P05979; -.
UniPathway; UPA00662; -.
EvolutionaryTrace; P05979; -.
PRO; PR:P05979; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0008144; F:drug binding; IDA:CAFA.
GO; GO:0020037; F:heme binding; IDA:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IMP:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0019371; P:cyclooxygenase pathway; IMP:CAFA.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
InterPro; IPR029580; COX-1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
PANTHER; PTHR11903:SF6; PTHR11903:SF6; 1.
Pfam; PF03098; An_peroxidase; 1.
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;
3D-structure; Complete proteome; Dioxygenase;
Direct protein sequencing; Disulfide bond; EGF-like domain;
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; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 24
CHAIN 25 600 Prostaglandin G/H synthase 1.
/FTId=PRO_0000023871.
TRANSMEM 74 82 Helical.
TRANSMEM 86 92 Helical.
TRANSMEM 97 105 Helical.
TRANSMEM 108 122 Helical.
DOMAIN 32 70 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 207 207 Proton acceptor.
ACT_SITE 385 385 For cyclooxygenase activity.
{ECO:0000269|PubMed:2122967}.
METAL 388 388 Iron (heme axial ligand).
SITE 104 104 Not glycosylated.
{ECO:0000269|PubMed:8349699}.
SITE 530 530 Aspirin-acetylated serine.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8349699}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8349699}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8349699}.
DISULFID 36 47
DISULFID 37 159
DISULFID 41 57
DISULFID 59 69
DISULFID 569 575
VARIANT 97 97 R -> H.
VARIANT 164 164 D -> G. {ECO:0000269|PubMed:2831188,
ECO:0000269|PubMed:3125548}.
VARIANT 456 456 R -> Q.
VARIANT 520 520 E -> K.
VARIANT 520 520 E -> Q.
VARIANT 525 525 M -> I.
MUTAGEN 385 385 Y->F: Abolishes cyclooxygenase activity.
{ECO:0000269|PubMed:2122967}.
CONFLICT 1 5 MSRQS -> MVQG (in Ref. 3; AAA31511).
{ECO:0000305}.
CONFLICT 193 193 S -> G (in Ref. 1; AAA31576 and 3;
AAA31511). {ECO:0000305}.
CONFLICT 540 540 C -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
HELIX 35 38 {ECO:0000244|PDB:1Q4G}.
STRAND 46 50 {ECO:0000244|PDB:1Q4G}.
TURN 51 53 {ECO:0000244|PDB:1Q4G}.
STRAND 54 58 {ECO:0000244|PDB:1Q4G}.
STRAND 62 65 {ECO:0000244|PDB:1Q4G}.
TURN 66 69 {ECO:0000244|PDB:1Q4G}.
HELIX 74 82 {ECO:0000244|PDB:1Q4G}.
HELIX 86 93 {ECO:0000244|PDB:1Q4G}.
HELIX 97 103 {ECO:0000244|PDB:1Q4G}.
HELIX 108 121 {ECO:0000244|PDB:1Q4G}.
STRAND 130 133 {ECO:0000244|PDB:1Q4G}.
STRAND 134 136 {ECO:0000244|PDB:1EQG}.
HELIX 139 143 {ECO:0000244|PDB:1Q4G}.
STRAND 149 152 {ECO:0000244|PDB:1Q4G}.
STRAND 159 161 {ECO:0000244|PDB:1EQG}.
STRAND 164 167 {ECO:0000244|PDB:1Q4G}.
HELIX 174 181 {ECO:0000244|PDB:1Q4G}.
HELIX 196 206 {ECO:0000244|PDB:1Q4G}.
TURN 207 209 {ECO:0000244|PDB:1Q4G}.
TURN 214 216 {ECO:0000244|PDB:1Q4G}.
STRAND 220 222 {ECO:0000244|PDB:1Q4G}.
STRAND 227 229 {ECO:0000244|PDB:1Q4G}.
HELIX 231 234 {ECO:0000244|PDB:1Q4G}.
HELIX 238 244 {ECO:0000244|PDB:1Q4G}.
STRAND 255 257 {ECO:0000244|PDB:1Q4G}.
STRAND 260 262 {ECO:0000244|PDB:1Q4G}.
TURN 266 268 {ECO:0000244|PDB:1Q4G}.
HELIX 281 283 {ECO:0000244|PDB:1Q4G}.
STRAND 288 291 {ECO:0000244|PDB:3KK6}.
HELIX 292 294 {ECO:0000244|PDB:1Q4G}.
HELIX 296 319 {ECO:0000244|PDB:1Q4G}.
HELIX 325 346 {ECO:0000244|PDB:1Q4G}.
HELIX 348 353 {ECO:0000244|PDB:1Q4G}.
HELIX 363 366 {ECO:0000244|PDB:1Q4G}.
STRAND 367 369 {ECO:0000244|PDB:1PGE}.
HELIX 379 384 {ECO:0000244|PDB:1Q4G}.
HELIX 388 390 {ECO:0000244|PDB:1Q4G}.
STRAND 393 397 {ECO:0000244|PDB:1Q4G}.
STRAND 400 402 {ECO:0000244|PDB:1Q4G}.
HELIX 404 407 {ECO:0000244|PDB:1Q4G}.
HELIX 413 417 {ECO:0000244|PDB:1Q4G}.
HELIX 419 428 {ECO:0000244|PDB:1Q4G}.
STRAND 434 438 {ECO:0000244|PDB:1Q4G}.
TURN 442 444 {ECO:0000244|PDB:1Q4G}.
HELIX 445 457 {ECO:0000244|PDB:1Q4G}.
HELIX 463 469 {ECO:0000244|PDB:1Q4G}.
HELIX 478 482 {ECO:0000244|PDB:1Q4G}.
STRAND 483 485 {ECO:0000244|PDB:1Q4G}.
HELIX 486 495 {ECO:0000244|PDB:1Q4G}.
HELIX 498 500 {ECO:0000244|PDB:1Q4G}.
HELIX 503 509 {ECO:0000244|PDB:1Q4G}.
STRAND 517 519 {ECO:0000244|PDB:2OYU}.
HELIX 520 535 {ECO:0000244|PDB:1Q4G}.
HELIX 538 540 {ECO:0000244|PDB:1Q4G}.
TURN 542 544 {ECO:0000244|PDB:1Q4G}.
HELIX 547 550 {ECO:0000244|PDB:1Q4G}.
HELIX 553 560 {ECO:0000244|PDB:1Q4G}.
HELIX 564 569 {ECO:0000244|PDB:1Q4G}.
STRAND 572 574 {ECO:0000244|PDB:1Q4G}.
SEQUENCE 600 AA; 68861 MW; 809887C7BB5A715C CRC64;
MSRQSISLRF PLLLLLLSPS PVFSADPGAP APVNPCCYYP CQHQGICVRF GLDRYQCDCT
RTGYSGPNCT IPEIWTWLRT TLRPSPSFIH FLLTHGRWLW DFVNATFIRD TLMRLVLTVR
SNLIPSPPTY NIAHDYISWE SFSNVSYYTR ILPSVPRDCP TPMDTKGKKQ LPDAEFLSRR
FLLRRKFIPD PQSTNLMFAF FAQHFTHQFF KTSGKMGPGF TKALGHGVDL GHIYGDNLER
QYQLRLFKDG KLKYQMLNGE VYPPSVEEAP VLMHYPRGIP PQSQMAVGQE VFGLLPGLML
YATIWLREHN RVCDLLKAEH PTWGDEQLFQ TARLILIGET IKIVIEEYVQ QLSGYFLQLK
FDPELLFGAQ FQYRNRIAME FNQLYHWHPL MPDSFRVGPQ DYSYEQFLFN TSMLVDYGVE
ALVDAFSRQP AGRIGGGRNI DHHILHVAVD VIKESRVLRL QPFNEYRKRF GMKPYTSFQE
LTGEKEMAAE LEELYGDIDA LEFYPGLLLE KCHPNSIFGE SMIEMGAPFS LKGLLGNPIC
SPEYWKASTF GGEVGFNLVK TATLKKLVCL NTKTCPYVSF HVPDPRQEDR PGVERPPTEL


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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
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
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
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
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
U0122m CLIA 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
U0699b CLIA 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
E0122r ELISA 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
E0122b ELISA 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
E0699b ELISA 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
U0699r CLIA 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
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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