Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Arachidonate 15-lipoxygenase (15-LOX) (EC 1.13.11.33) (12/15-lipoxygenase) (Arachidonate 12-lipoxygenase, leukocyte-type) (12-LOX) (L-12LO) (EC 1.13.11.31) (Arachidonate omega-6 lipoxygenase) (Erythroid cell-specific 15-lipoxygenase)

 LOX15_RABIT             Reviewed;         663 AA.
P12530; O19043;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
15-FEB-2017, entry version 139.
RecName: Full=Arachidonate 15-lipoxygenase;
Short=15-LOX;
EC=1.13.11.33 {ECO:0000269|PubMed:9414270, ECO:0000269|PubMed:9600854};
AltName: Full=12/15-lipoxygenase;
AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type;
Short=12-LOX;
Short=L-12LO;
EC=1.13.11.31 {ECO:0000269|PubMed:9600854};
AltName: Full=Arachidonate omega-6 lipoxygenase;
AltName: Full=Erythroid cell-specific 15-lipoxygenase;
Name=ALOX15;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2612916; DOI=10.1016/0378-1119(89)90526-X;
O'Prey J., Chester J., Thiele B.J., Janetzki S., Prehn S., Fleming J.,
Harrison P.R.;
"The promoter structure and complete sequence of the gene encoding the
rabbit erythroid cell-specific 15-lipoxygenase.";
Gene 84:493-499(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
MUTAGENESIS OF PHE-353.
PubMed=9600854; DOI=10.1006/jmbi.1998.1737;
Berger M., Schwarz K., Thiele H., Reimann I., Huth A., Borngraeber S.,
Kuehn H., Thiele B.-J.;
"Simultaneous expression of leukocyte-type 12-lipoxygenase and
reticulocyte-type 15-lipoxygenase in rabbits.";
J. Mol. Biol. 278:935-948(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-31.
PubMed=2777088; DOI=10.1016/0378-1119(89)90103-0;
Fleming J., Thiele B.J., Chester J., O'Prey J., Janetzki S.,
Aitken A., Anton I.A., Rapoport S.M., Harrison P.R.;
"The complete sequence of the rabbit erythroid cell-specific 15-
lipoxygenase mRNA: comparison of the predicted amino acid sequence of
the erythrocyte lipoxygenase with other lipoxygenases.";
Gene 79:181-188(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
PubMed=3123326; DOI=10.1016/0378-1119(87)90182-X;
Thiele B.J., Fleming J., Kasturi K., O'Prey J., Black E., Chester J.,
Rapoport S.M., Harrison P.R.;
"Cloning of a rabbit erythroid-cell-specific lipoxygenase mRNA.";
Gene 57:111-119(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND GENE STRUCTURE.
PubMed=2386503;
Thiele B.J., Fleming J., Chester J., O'Prey J., Prehn S., Janetzki S.,
Rapoport S.M., Harrison P.R.;
"Structure of the mRNA and of the gene coding for the rabbit erythroid
15-lipoxygenase.";
Biomed. Biochim. Acta 49:S17-S24(1990).
[6]
CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=9414270;
Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G.,
Kuehn H.;
"Membrane translocation of 15-lipoxygenase in hematopoietic cells is
calcium-dependent and activates the oxygenase activity of the
enzyme.";
Blood 91:64-74(1998).
[7]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON AND
SUBSTRATE ANALOG.
PubMed=9406550; DOI=10.1038/nsb1297-1003;
Gillmor S.A., Villasenor A., Fletterick R., Sigal E., Browner M.F.;
"The structure of mammalian 15-lipoxygenase reveals similarity to the
lipases and the determinants of substrate specificity.";
Nat. Struct. Biol. 4:1003-1009(1997).
-!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the
stereo-specific peroxidation of free and esterified
polyunsaturated fatty acids generating a spectrum of bioactive
lipid mediators. Converts arachidonic acid into 12-
hydroperoxyeicosatetraenoic acid/12-HPETE and 15-
hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic
acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-
hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin
A3. Probably plays an important role in the immune and
inflammatory responses. Through the oxygenation of membrane-bound
phosphatidylethanolamine in macrophages may favor clearance of
apoptotic cells during inflammation by resident macrophages and
prevent an autoimmune response associated with the clearance of
apoptotic cells by inflammatory monocytes. In parallel, may
regulate actin polymerization which is crucial for several
biological processes, including macrophage function. May also
regulate macrophage function through regulation of the peroxisome
proliferator activated receptor signaling pathway. Finally, it is
also involved in the cellular response to IL13/interleukin-13. In
addition to its role in the immune and inflammatory responses, may
play a role in epithelial wound healing in the cornea maybe
through production of lipoxin A4. May also play a role in
endoplasmic reticulum stress response and the regulation of bone
mass. {ECO:0000269|PubMed:9414270, ECO:0000269|PubMed:9600854}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-
12-hydroperoxyicosa-5,8,10,14-tetraenoate.
{ECO:0000269|PubMed:9600854}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-
15-hydroperoxyicosa-5,8,11,13-tetraenoate.
{ECO:0000269|PubMed:9414270, ECO:0000269|PubMed:9600854}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Note=Binds 1 Fe cation per subunit.;
-!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
biosynthesis. {ECO:0000269|PubMed:9600854}.
-!- SUBUNIT: Interacts with PEBP1; in response to IL13/interleukin-13,
prevents the interaction of PEBP1 with RAF1 to activate the ERK
signaling cascade. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:9414270}. Cell membrane
{ECO:0000269|PubMed:9414270}; Peripheral membrane protein
{ECO:0000269|PubMed:9414270}. Lipid droplet {ECO:0000250}.
Note=Translocates from the cytosol to the plasma membrane when
stimulated by IL13/interleukin-13 and in macrophages binding
apoptotic cells (By similarity). Predominantly cytosolic; becomes
enriched at membranes upon calcium binding. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in reticulocytes (at protein level).
{ECO:0000269|PubMed:9414270}.
-!- DOMAIN: The PLAT domain can bind calcium ions; this promotes
association with membranes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-!- CAUTION: According to the authors the mRNA described in
PubMed:9600854 may be encoded by a gene different from ALOX15.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M33291; AAA75014.1; -; Genomic_DNA.
EMBL; Z97654; CAB10746.1; -; mRNA.
EMBL; M27214; AAB86978.1; -; mRNA.
EMBL; M22617; AAA31385.1; -; mRNA.
PIR; JQ0018; JQ0018.
RefSeq; NP_001075751.1; NM_001082282.1.
RefSeq; NP_001139620.1; NM_001146148.1.
UniGene; Ocu.2185; -.
UniGene; Ocu.7470; -.
PDB; 1LOX; X-ray; 2.40 A; A=2-663.
PDB; 2P0M; X-ray; 2.40 A; A/B=2-663.
PDBsum; 1LOX; -.
PDBsum; 2P0M; -.
ProteinModelPortal; P12530; -.
SMR; P12530; -.
STRING; 9986.ENSOCUP00000017072; -.
BindingDB; P12530; -.
ChEMBL; CHEMBL4358; -.
SwissLipids; SLP:000001603; -.
GeneID; 100009114; -.
GeneID; 100271999; -.
KEGG; ocu:100009114; -.
KEGG; ocu:100271999; -.
CTD; 239; -.
CTD; 246; -.
eggNOG; ENOG410IKAN; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
HOGENOM; HOG000234358; -.
HOVERGEN; HBG005150; -.
InParanoid; P12530; -.
KO; K00460; -.
BRENDA; 1.13.11.33; 1749.
UniPathway; UPA00881; -.
EvolutionaryTrace; P12530; -.
PRO; PR:P12530; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0005811; C:lipid particle; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:UniProtKB.
GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0035963; P:cellular response to interleukin-13; ISS:UniProtKB.
GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
GO; GO:2001303; P:lipoxin A4 biosynthetic process; ISS:UniProtKB.
GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB.
GO; GO:0002820; P:negative regulation of adaptive immune response; ISS:UniProtKB.
GO; GO:0001503; P:ossification; ISS:UniProtKB.
GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:1901074; P:regulation of engulfment of apoptotic cell; ISS:UniProtKB.
GO; GO:0035358; P:regulation of peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; ISS:UniProtKB.
Gene3D; 2.60.60.20; -; 1.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001885; LipOase_mml.
InterPro; IPR001024; PLAT/LH2_dom.
PANTHER; PTHR11771; PTHR11771; 1.
Pfam; PF00305; Lipoxygenase; 1.
Pfam; PF01477; PLAT; 1.
PRINTS; PR00087; LIPOXYGENASE.
PRINTS; PR00467; MAMLPOXGNASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF48484; SSF48484; 1.
SUPFAM; SSF49723; SSF49723; 1.
PROSITE; PS00711; LIPOXYGENASE_1; 1.
PROSITE; PS00081; LIPOXYGENASE_2; 1.
PROSITE; PS51393; LIPOXYGENASE_3; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Complete proteome; Cytoplasm;
Dioxygenase; Direct protein sequencing; Fatty acid metabolism; Iron;
Lipid droplet; Lipid metabolism; Lipid-binding; Membrane;
Metal-binding; Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2777088}.
CHAIN 2 663 Arachidonate 15-lipoxygenase.
/FTId=PRO_0000220699.
DOMAIN 2 115 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 116 663 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 361 361 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:9406550}.
METAL 366 366 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:9406550}.
METAL 541 541 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:9406550}.
METAL 545 545 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:9406550}.
METAL 663 663 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726,
ECO:0000269|PubMed:9406550}.
MUTAGEN 353 353 F->L: Changes the stereoselectivity of
the oxygenation reaction to produce
(12S)-HPETE instead of (15S)-HPETE.
{ECO:0000269|PubMed:9600854}.
CONFLICT 42 42 T -> S (in Ref. 2; CAB10746).
{ECO:0000305}.
CONFLICT 64 64 R -> K (in Ref. 2; CAB10746).
{ECO:0000305}.
CONFLICT 190 190 N -> D (in Ref. 3; AAB86978).
{ECO:0000305}.
CONFLICT 194 194 I -> V (in Ref. 3; AAB86978).
{ECO:0000305}.
CONFLICT 353 353 F -> L (in Ref. 2; CAB10746).
{ECO:0000305}.
STRAND 3 10 {ECO:0000244|PDB:1LOX}.
STRAND 12 15 {ECO:0000244|PDB:2P0M}.
STRAND 19 30 {ECO:0000244|PDB:1LOX}.
STRAND 32 39 {ECO:0000244|PDB:1LOX}.
STRAND 46 52 {ECO:0000244|PDB:1LOX}.
STRAND 59 68 {ECO:0000244|PDB:1LOX}.
STRAND 70 72 {ECO:0000244|PDB:1LOX}.
STRAND 76 88 {ECO:0000244|PDB:1LOX}.
STRAND 93 101 {ECO:0000244|PDB:1LOX}.
STRAND 103 105 {ECO:0000244|PDB:2P0M}.
STRAND 107 110 {ECO:0000244|PDB:1LOX}.
HELIX 126 139 {ECO:0000244|PDB:1LOX}.
STRAND 152 154 {ECO:0000244|PDB:1LOX}.
HELIX 158 160 {ECO:0000244|PDB:1LOX}.
HELIX 163 165 {ECO:0000244|PDB:1LOX}.
HELIX 169 175 {ECO:0000244|PDB:1LOX}.
HELIX 189 192 {ECO:0000244|PDB:1LOX}.
HELIX 193 195 {ECO:0000244|PDB:1LOX}.
HELIX 201 206 {ECO:0000244|PDB:1LOX}.
HELIX 214 222 {ECO:0000244|PDB:1LOX}.
HELIX 226 235 {ECO:0000244|PDB:1LOX}.
HELIX 259 270 {ECO:0000244|PDB:1LOX}.
STRAND 274 278 {ECO:0000244|PDB:1LOX}.
HELIX 280 282 {ECO:0000244|PDB:1LOX}.
STRAND 301 306 {ECO:0000244|PDB:1LOX}.
TURN 308 310 {ECO:0000244|PDB:2P0M}.
STRAND 312 318 {ECO:0000244|PDB:1LOX}.
HELIX 338 358 {ECO:0000244|PDB:1LOX}.
HELIX 359 365 {ECO:0000244|PDB:1LOX}.
HELIX 366 379 {ECO:0000244|PDB:1LOX}.
HELIX 385 390 {ECO:0000244|PDB:1LOX}.
HELIX 391 394 {ECO:0000244|PDB:1LOX}.
HELIX 397 404 {ECO:0000244|PDB:1LOX}.
TURN 405 408 {ECO:0000244|PDB:1LOX}.
HELIX 414 418 {ECO:0000244|PDB:1LOX}.
TURN 420 424 {ECO:0000244|PDB:1LOX}.
HELIX 425 434 {ECO:0000244|PDB:1LOX}.
HELIX 439 442 {ECO:0000244|PDB:1LOX}.
HELIX 444 450 {ECO:0000244|PDB:1LOX}.
HELIX 460 480 {ECO:0000244|PDB:1LOX}.
TURN 481 483 {ECO:0000244|PDB:1LOX}.
HELIX 487 491 {ECO:0000244|PDB:1LOX}.
HELIX 494 504 {ECO:0000244|PDB:1LOX}.
TURN 505 509 {ECO:0000244|PDB:1LOX}.
HELIX 511 514 {ECO:0000244|PDB:1LOX}.
HELIX 523 536 {ECO:0000244|PDB:1LOX}.
HELIX 539 545 {ECO:0000244|PDB:1LOX}.
HELIX 548 551 {ECO:0000244|PDB:1LOX}.
STRAND 552 554 {ECO:0000244|PDB:1LOX}.
HELIX 555 557 {ECO:0000244|PDB:1LOX}.
STRAND 568 570 {ECO:0000244|PDB:1LOX}.
HELIX 574 580 {ECO:0000244|PDB:1LOX}.
HELIX 584 596 {ECO:0000244|PDB:1LOX}.
HELIX 618 643 {ECO:0000244|PDB:1LOX}.
STRAND 645 647 {ECO:0000244|PDB:1LOX}.
TURN 654 656 {ECO:0000244|PDB:1LOX}.
STRAND 657 660 {ECO:0000244|PDB:1LOX}.
SEQUENCE 663 AA; 75310 MW; C3391E1E6E7930BF CRC64;
MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PTRNKEEEFK VNVSKYLGSL
LFVRLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW VVGDGVQSLP VGTGCTTVGD
PQGLFQKHRE QELEERRKLY QWGSWKEGLI LNVAGSKLTD LPVDERFLED KKIDFEASLA
WGLAELALKN SLNILAPWKT LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM
LLRRSVQLPA RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP
LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS SDFQVHELNS
HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI NVRARNGLVS DFGIFDQIMS
TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD RGLLGVESSF YAQDALRLWE IISRYVQGIM
GLYYKTDEAV RDDLELQSWC REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ
HSSIHLGQLD WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD
QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE YLRPSIVENS
VAI


Related products :

Catalog number Product name Quantity
E0891Rb ELISA kit 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
U0891Rb CLIA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E0891Rb ELISA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E1356m ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
E1356m ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
U1356m CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
E1356h ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
E1356h ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
U1356h CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
U1356r CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
E1356r ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
E1356r ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
E0891h ELISA kit 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Arachidonate omega-6 lipoxygenase,Homo sapiens,Human,LOG15 96T
E0891h ELISA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Arachidonate omega-6 lipoxygenase,Homo sapiens,Human,LOG15 96T
U0891h CLIA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Arachidonate omega-6 lipoxygenase,Homo sapiens,Human,LOG15 96T
U1965h CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
E1965h ELISA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
E1965h ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
U1965h CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
E1965m ELISA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
U1965m CLIA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1965m ELISA 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
U1965m CLIA 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1965b ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
U1965b CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur