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

 LOX15_MOUSE             Reviewed;         663 AA.
P39654; Q4FJY9; Q5F2E3; Q6PHB2;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 4.
25-OCT-2017, entry version 150.
RecName: Full=Arachidonate 15-lipoxygenase;
Short=15-LOX;
EC=1.13.11.33 {ECO:0000269|PubMed:8188678};
AltName: Full=12/15-lipoxygenase;
Short=12/15-LO;
AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type;
Short=12-LOX;
Short=L-12LO;
EC=1.13.11.31 {ECO:0000269|PubMed:8188678};
AltName: Full=Arachidonate omega-6 lipoxygenase;
Name=Alox15; Synonyms=Alox12l;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J, and ICR; TISSUE=Spleen;
PubMed=8188678;
Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.;
"cDNA cloning, expression, mutagenesis of C-terminal isoleucine,
genomic structure, and chromosomal localizations of murine 12-
lipoxygenases.";
J. Biol. Chem. 269:13979-13987(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=7811740; DOI=10.1016/0005-2760(94)00199-9;
Freire-Moar J., Alavi-Nassab A., Ng M., Mulkins M., Sigal E.;
"Cloning and characterization of a murine macrophage lipoxygenase.";
Biochim. Biophys. Acta 1254:112-116(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=8798642; DOI=10.1074/jbc.271.39.24278;
Sun D., Funk C.D.;
"Disruption of 12/15-lipoxygenase expression in peritoneal
macrophages. Enhanced utilization of the 5-lipoxygenase pathway and
diminished oxidation of low density lipoprotein.";
J. Biol. Chem. 271:24055-24062(1996).
[8]
FUNCTION IN MACROPHAGE.
PubMed=10432118; DOI=10.1038/22572;
Huang J.T., Welch J.S., Ricote M., Binder C.J., Willson T.M.,
Kelly C., Witztum J.L., Funk C.D., Conrad D., Glass C.K.;
"Interleukin-4-dependent production of PPAR-gamma ligands in
macrophages by 12/15-lipoxygenase.";
Nature 400:378-382(1999).
[9]
FUNCTION IN ACTIN REGULATION, AND SUBCELLULAR LOCATION.
PubMed=11278875; DOI=10.1074/jbc.M011276200;
Miller Y.I., Chang M.K., Funk C.D., Feramisco J.R., Witztum J.L.;
"12/15-lipoxygenase translocation enhances site-specific actin
polymerization in macrophages phagocytosing apoptotic cells.";
J. Biol. Chem. 276:19431-19439(2001).
[10]
FUNCTION IN BONE DEVELOPMENT, AND DISRUPTION PHENOTYPE.
PubMed=14716014; DOI=10.1126/science.1090985;
Klein R.F., Allard J., Avnur Z., Nikolcheva T., Rotstein D.,
Carlos A.S., Shea M., Waters R.V., Belknap J.K., Peltz G.,
Orwoll E.S.;
"Regulation of bone mass in mice by the lipoxygenase gene Alox15.";
Science 303:229-232(2004).
[11]
FUNCTION IN HEALING, AND TISSUE SPECIFICITY.
PubMed=15708862; DOI=10.1074/jbc.M410638200;
Gronert K., Maheshwari N., Khan N., Hassan I.R., Dunn M.,
Laniado Schwartzman M.;
"A role for the mouse 12/15-lipoxygenase pathway in promoting
epithelial wound healing and host defense.";
J. Biol. Chem. 280:15267-15278(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION IN ER STRESS RESPONSE, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=22215650; DOI=10.1152/ajpendo.00373.2011;
Cole B.K., Kuhn N.S., Green-Mitchell S.M., Leone K.A., Raab R.M.,
Nadler J.L., Chakrabarti S.K.;
"12/15-Lipoxygenase signaling in the endoplasmic reticulum stress
response.";
Am. J. Physiol. 302:E654-E665(2012).
[14]
FUNCTION IN APOPTOTIC CELL CLEARANCE, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=22503541; DOI=10.1016/j.immuni.2012.03.010;
Uderhardt S., Herrmann M., Oskolkova O.V., Aschermann S., Bicker W.,
Ipseiz N., Sarter K., Frey B., Rothe T., Voll R., Nimmerjahn F.,
Bochkov V.N., Schett G., Kroenke G.;
"12/15-lipoxygenase orchestrates the clearance of apoptotic cells and
maintains immunologic tolerance.";
Immunity 36:834-846(2012).
-!- 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:10432118, ECO:0000269|PubMed:11278875,
ECO:0000269|PubMed:14716014, ECO:0000269|PubMed:15708862,
ECO:0000269|PubMed:22215650, ECO:0000269|PubMed:22503541}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-
12-hydroperoxyicosa-5,8,10,14-tetraenoate.
{ECO:0000269|PubMed:8188678}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-
15-hydroperoxyicosa-5,8,11,13-tetraenoate.
{ECO:0000269|PubMed:8188678}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Note=Binds 1 Fe cation per subunit.;
-!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
biosynthesis.
-!- SUBUNIT: Interacts with PEBP1; in response to IL13/interleukin-13,
prevents the interaction of PEBP1 with RAF1 to activate the ERK
signaling cascade. {ECO:0007001}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11278875}. Cell membrane
{ECO:0000269|PubMed:11278875}; Peripheral membrane protein
{ECO:0000269|PubMed:11278875}. Lipid droplet {ECO:0007001}.
Note=Predominantly cytosolic; becomes enriched at membranes upon
calcium binding. Translocates from the cytosol to the plasma
membrane when stimulated by IL13/interleukin-13 and in macrophages
binding apoptotic cells.
-!- TISSUE SPECIFICITY: Found in pituitary and pineal glands as well
as leukocytes, kidney, aorta, small intestine and cornea. Also
expressed by resident peritoneal macrophages (at protein level).
{ECO:0000269|PubMed:15708862, ECO:0000269|PubMed:22503541,
ECO:0000269|PubMed:8188678, ECO:0000269|PubMed:8798642}.
-!- INDUCTION: Up-regulated in response to endoplasmic reticulum
stress (at protein level). {ECO:0000269|PubMed:22215650}.
-!- DOMAIN: The PLAT domain can bind calcium ions; this promotes
association with membranes. {ECO:0007001}.
-!- DISRUPTION PHENOTYPE: Mice are fertile and do not display overt
phenotype. However, reduced endoplasmic reticulum stress response
to high-fat diet is observed. Aged mice also display systemic
autoimmunity, a significant and spontaneous production of several
forms of autoantibodies being detected and glomerulonephritis and
deposits of complement and immunoglobulins within their glomeruli
being observed. They also display reduced bone mass.
{ECO:0000269|PubMed:14716014, ECO:0000269|PubMed:22215650,
ECO:0000269|PubMed:22503541, ECO:0000269|PubMed:8798642}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000320}.
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EMBL; U04331; AAA20658.1; -; mRNA.
EMBL; L34570; AAA64930.1; -; mRNA.
EMBL; AK142371; BAE25045.1; -; mRNA.
EMBL; CT010263; CAJ18471.1; -; mRNA.
EMBL; AL596096; CAI51979.1; -; Genomic_DNA.
EMBL; BC056625; AAH56625.1; -; mRNA.
EMBL; BC081546; AAH81546.1; -; mRNA.
CCDS; CCDS24944.1; -.
PIR; B54075; B54075.
RefSeq; NP_033790.3; NM_009660.3.
UniGene; Mm.4584; -.
ProteinModelPortal; P39654; -.
SMR; P39654; -.
STRING; 10090.ENSMUSP00000019068; -.
BindingDB; P39654; -.
ChEMBL; CHEMBL3259476; -.
SwissLipids; SLP:000001638; -.
PhosphoSitePlus; P39654; -.
MaxQB; P39654; -.
PaxDb; P39654; -.
PRIDE; P39654; -.
Ensembl; ENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924.
GeneID; 11687; -.
KEGG; mmu:11687; -.
UCSC; uc007juo.1; mouse.
CTD; 246; -.
MGI; MGI:87997; Alox15.
eggNOG; ENOG410IKAN; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
GeneTree; ENSGT00550000074415; -.
HOGENOM; HOG000234358; -.
HOVERGEN; HBG005150; -.
InParanoid; P39654; -.
KO; K00460; -.
OMA; LTCWKDL; -.
OrthoDB; EOG091G04A4; -.
PhylomeDB; P39654; -.
TreeFam; TF105320; -.
BRENDA; 1.13.11.31; 3474.
Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-MMU-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathway; UPA00881; -.
PRO; PR:P39654; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018924; -.
CleanEx; MM_ALOX15; -.
ExpressionAtlas; P39654; baseline and differential.
Genevisible; P39654; MM.
GO; GO:0005737; C:cytoplasm; HTP:MGI.
GO; GO:0005829; C:cytosol; HTP:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; HMP:UniProtKB.
GO; GO:0005811; C:lipid droplet; HMP:UniProtKB.
GO; GO:0016020; C:membrane; HMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; HTP:UniProtKB.
GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; HTP:UniProtKB.
GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; HTP:UniProtKB.
GO; GO:0051120; F:hepoxilin A3 synthase activity; RCA:Ensembl.
GO; GO:0047977; F:hepoxilin-epoxide hydrolase activity; RCA:Ensembl.
GO; GO:0005506; F:iron ion binding; HMP:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; HMP:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; HDA:UniProtKB.
GO; GO:0019369; P:arachidonic acid metabolic process; HTP:UniProtKB.
GO; GO:0030282; P:bone mineralization; HDA:MGI.
GO; GO:0071277; P:cellular response to calcium ion; HMP:UniProtKB.
GO; GO:0035963; P:cellular response to interleukin-13; HMP:UniProtKB.
GO; GO:0051122; P:hepoxilin biosynthetic process; HMP:UniProtKB.
GO; GO:2001303; P:lipoxin A4 biosynthetic process; HDA:UniProtKB.
GO; GO:0019372; P:lipoxygenase pathway; HTP:UniProtKB.
GO; GO:0002820; P:negative regulation of adaptive immune response; HDA:UniProtKB.
GO; GO:0001503; P:ossification; HDA:MGI.
GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; HDA:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; HDA:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; HMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; HMP:UniProtKB.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; RCA:Ensembl.
GO; GO:1901074; P:regulation of engulfment of apoptotic cell; HDA:UniProtKB.
GO; GO:0035358; P:regulation of peroxisome proliferator activated receptor signaling pathway; HDA:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; HDA:UniProtKB.
GO; GO:0042060; P:wound healing; HDA:UniProtKB.
Gene3D; 2.60.60.20; -; 1.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR036226; LipOase_C_sf.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001885; LipOase_mml.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
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;
Calcium; Cell membrane; Complete proteome; Cytoplasm; Dioxygenase;
Fatty acid metabolism; Iron; Lipid droplet; Lipid metabolism;
Lipid-binding; Membrane; Metal-binding; Oxidoreductase;
Reference proteome.
CHAIN 1 663 Arachidonate 15-lipoxygenase.
/FTId=PRO_0000220686.
DOMAIN 2 115 PLAT. {ECO:0000270|PROSITE-
ProRule:PRU00152}.
DOMAIN 116 663 Lipoxygenase. {ECO:0000270|PROSITE-
ProRule:PRU00726}.
METAL 361 361 Iron; catalytic. {ECO:0000270|PROSITE-
ProRule:PRU00726}.
METAL 366 366 Iron; catalytic. {ECO:0000270|PROSITE-
ProRule:PRU00726}.
METAL 541 541 Iron; catalytic. {ECO:0000270|PROSITE-
ProRule:PRU00726}.
METAL 545 545 Iron; catalytic. {ECO:0000270|PROSITE-
ProRule:PRU00726}.
METAL 663 663 Iron; via carboxylate; catalytic.
{ECO:0000270|PROSITE-ProRule:PRU00726}.
CONFLICT 37 37 K -> N (in Ref. 2; AAA64930).
{ECO:0000320}.
CONFLICT 119 119 E -> Q (in Ref. 2; AAA64930).
{ECO:0000320}.
CONFLICT 397 397 T -> N (in Ref. 2; AAA64930).
{ECO:0000320}.
CONFLICT 568 568 K -> T (in Ref. 4; CAJ18471 and 6;
AAH56625/AAH81546). {ECO:0000320}.
SEQUENCE 663 AA; 75445 MW; 0D5412B4502B5799 CRC64;
MGVYRIRVST GDSVYAGSNN EVYLWLIGQH GEASLGKLFR PCRNSEAEFK VDVSEYLGPL
LFVRVQKWHY LKEDAWFCNW ISVKGPGDQG SEYTFPCYRW VQGTSILNLP EGTGCTVVED
SQGLFRNHRE EELEERRSLY RWGNWKDGTI LNVAATSISD LPVDQRFRED KRLEFEASQV
LGTMDTVINF PKNTVTCWKS LDDFNYVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM
VLKRSTCLPA RLVFPPGMEK LQAQLDEELK KGTLFEADFF LLDGIKANVI LCSQQYLAAP
LVMLKLQPDG QLLPIAIQLE LPKTGSTPPP IFTPLDPPMD WLLAKCWVRS SDLQLHELQA
HLLRGHLVAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI NVRARSDLIS ERGFFDKVMS
TGGGGHLDLL KQAGAFLTYS SLCPPDDLAE RGLLDIDTCF YAKDALQLWQ VMNRYVVGMF
DLYYKTDQAV QDDYELQSWC QEITEIGLQG AQDRGFPTSL QSRAQACHFI TMCIFTCTAQ
HSSIHLGQLD WFYWVPNAPC TMRLPPPKTK DATMEKLMAT LPNPNQSTLQ INVVWLLGRR
QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE YLRPSLVENS
VAI


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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
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 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
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
E0891Rb ELISA 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 kit 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E1965h ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 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
U1965h CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,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 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
U1965b CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
E1965b ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T


 

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