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) (EC 1.13.11.31) (Arachidonate omega-6 lipoxygenase) (Erythroid cell-specific 15-lipoxygenase)

 LOX15_PIG               Reviewed;         663 AA.
P16469; F1RFT4;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 3.
30-AUG-2017, entry version 138.
RecName: Full=Arachidonate 15-lipoxygenase;
Short=15-LOX;
EC=1.13.11.33 {ECO:0000269|PubMed:8305485};
AltName: Full=12/15-lipoxygenase;
AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type;
Short=12-LOX;
EC=1.13.11.31 {ECO:0000269|PubMed:8305485};
AltName: Full=Arachidonate omega-6 lipoxygenase;
AltName: Full=Erythroid cell-specific 15-lipoxygenase;
Name=ALOX15;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Leukocyte;
PubMed=2315307; DOI=10.1073/pnas.87.6.2142;
Yoshimoto T., Suzuki H., Yamamoto S., Takai T., Yokoyama C.,
Tanabe T.;
"Cloning and sequence analysis of the cDNA for arachidonate 12-
lipoxygenase of porcine leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 87:2142-2146(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1601885;
Arakawa T., Oshima T., Kishimoto K., Yoshimoto T., Yamamoto S.;
"Molecular structure and function of the porcine arachidonate 12-
lipoxygenase gene.";
J. Biol. Chem. 267:12188-12191(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Porcine genome sequencing project;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, IRON-BINDING, AND
MUTAGENESIS OF ILE-106; HIS-128; HIS-356; HIS-361; HIS-366; HIS-384;
HIS-393; MET-398; VAL-418; VAL-419; HIS-426; CYS-533 AND HIS-541.
PubMed=8305485; DOI=10.1016/0005-2760(94)90234-8;
Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F.,
Ebina Y., Miyatake A., Tanabe T.;
"Site-directed mutagenesis studies on the iron-binding domain and the
determinant for the substrate oxygenation site of porcine leukocyte
arachidonate 12-lipoxygenase.";
Biochim. Biophys. Acta 1210:308-316(1994).
[5]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 112-663 IN COMPLEX WITH
INHIBITOR, AND IRON-BINDING.
PubMed=22795085; DOI=10.1016/j.str.2012.06.003;
Xu S., Mueser T.C., Marnett L.J., Funk M.O. Jr.;
"Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor
complex identifies a substrate-binding channel for catalysis.";
Structure 20:1490-1497(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:8305485}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-
12-hydroperoxyicosa-5,8,10,14-tetraenoate.
{ECO:0000269|PubMed:8305485}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-
15-hydroperoxyicosa-5,8,11,13-tetraenoate.
{ECO:0000269|PubMed:8305485}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00726,
ECO:0000269|PubMed:8305485};
Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00726, ECO:0000269|PubMed:8305485};
-!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
biosynthesis. {ECO:0000269|PubMed:8305485}.
-!- 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:0000250}. Cell
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Lipid droplet {ECO:0000250}. 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 (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Leukocytes, pituitary gland, lung and in very
small amount in jejunum and spleen.
-!- DOMAIN: The PLAT domain can bind calcium ions; this promotes
association with membranes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M31417; AAA31068.1; -; mRNA.
EMBL; D10621; BAA01471.1; -; Genomic_DNA.
EMBL; CU972403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A35087; A35087.
RefSeq; NP_999096.1; NM_213931.1.
UniGene; Ssc.10974; -.
PDB; 3RDE; X-ray; 1.89 A; A/B/C/D=112-663.
PDBsum; 3RDE; -.
SMR; P16469; -.
STRING; 9823.ENSSSCP00000018988; -.
BindingDB; P16469; -.
ChEMBL; CHEMBL2381; -.
SwissLipids; SLP:000001604; -.
PaxDb; P16469; -.
PeptideAtlas; P16469; -.
PRIDE; P16469; -.
Ensembl; ENSSSCT00000019506; ENSSSCP00000018988; ENSSSCG00000017923.
GeneID; 396971; -.
KEGG; ssc:396971; -.
CTD; 246; -.
eggNOG; ENOG410IKAN; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
GeneTree; ENSGT00550000074415; -.
HOGENOM; HOG000234358; -.
HOVERGEN; HBG005150; -.
InParanoid; P16469; -.
KO; K00460; -.
OMA; LTCWKDL; -.
OrthoDB; EOG091G04A4; -.
TreeFam; TF105320; -.
BRENDA; 1.13.11.31; 6170.
Reactome; R-SSC-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-SSC-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-SSC-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
SABIO-RK; P16469; -.
UniPathway; UPA00881; -.
Proteomes; UP000008227; Chromosome 12.
Bgee; ENSSSCG00000017923; -.
ExpressionAtlas; P16469; differential.
Genevisible; P16469; SS.
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; IDA: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: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.
CHAIN 1 663 Arachidonate 15-lipoxygenase.
/FTId=PRO_0000220684.
DOMAIN 2 115 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 116 663 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 361 361 Iron; catalytic.
METAL 366 366 Iron; catalytic.
METAL 541 541 Iron; catalytic.
METAL 545 545 Iron; catalytic.
METAL 663 663 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
MUTAGEN 106 106 I->V: No effect on the stereoselectivity
of the oxygenation reaction.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 128 128 H->L: No specific effect on enzymatic
activity and iron-binding.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 356 356 H->L: No specific effect on enzymatic
activity and iron-binding.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 361 361 H->L,Q: Loss of enzymatic activity and
iron-binding.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 366 366 H->L: Loss of enzymatic activity and
iron-binding.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 384 384 H->L: Labile enzyme with normal enzymatic
activity. {ECO:0000269|PubMed:8305485}.
MUTAGEN 393 393 H->L: Labile enzyme with loss of
enzymatic activity.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 398 398 M->L: No effect on the stereoselectivity
of the oxygenation reaction.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 418 418 V->I: Alters the stereoselectivity of the
oxygenation reaction. Changes the
stereoselectivity of the oxygenation
toward the production of (15S)-HPETE;
when associated with M-419.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 419 419 V->M: Alters the stereoselectivity of the
oxygenation reaction. Changes the
stereoselectivity of the oxygenation
toward the production of (15S)-HPETE;
when associated with I-418.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 426 426 H->L: Decreased enzymatic activity
without effect on iron-binding.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 533 533 C->S: No specific effect on enzymatic
activity and iron-binding.
{ECO:0000269|PubMed:8305485}.
MUTAGEN 541 541 H->L: Loss of enzymatic activity and
iron-binding.
{ECO:0000269|PubMed:8305485}.
CONFLICT 218 218 R -> Q (in Ref. 1; AAA31068/BAA01471).
{ECO:0000305}.
CONFLICT 323 323 H -> R (in Ref. 1; AAA31068/BAA01471).
{ECO:0000305}.
CONFLICT 494 494 L -> F (in Ref. 1; AAA31068/BAA01471).
{ECO:0000305}.
CONFLICT 553 553 S -> T (in Ref. 1; AAA31068/BAA01471).
{ECO:0000305}.
CONFLICT 623 623 V -> G (in Ref. 1; BAA01471).
{ECO:0000305}.
HELIX 126 139 {ECO:0000244|PDB:3RDE}.
HELIX 158 160 {ECO:0000244|PDB:3RDE}.
HELIX 163 165 {ECO:0000244|PDB:3RDE}.
HELIX 169 193 {ECO:0000244|PDB:3RDE}.
HELIX 201 207 {ECO:0000244|PDB:3RDE}.
HELIX 214 222 {ECO:0000244|PDB:3RDE}.
HELIX 226 235 {ECO:0000244|PDB:3RDE}.
HELIX 259 270 {ECO:0000244|PDB:3RDE}.
STRAND 274 278 {ECO:0000244|PDB:3RDE}.
HELIX 280 282 {ECO:0000244|PDB:3RDE}.
STRAND 301 306 {ECO:0000244|PDB:3RDE}.
STRAND 312 318 {ECO:0000244|PDB:3RDE}.
HELIX 338 358 {ECO:0000244|PDB:3RDE}.
HELIX 359 365 {ECO:0000244|PDB:3RDE}.
HELIX 366 379 {ECO:0000244|PDB:3RDE}.
HELIX 385 390 {ECO:0000244|PDB:3RDE}.
HELIX 391 394 {ECO:0000244|PDB:3RDE}.
HELIX 397 407 {ECO:0000244|PDB:3RDE}.
HELIX 414 418 {ECO:0000244|PDB:3RDE}.
TURN 420 424 {ECO:0000244|PDB:3RDE}.
HELIX 425 436 {ECO:0000244|PDB:3RDE}.
HELIX 440 442 {ECO:0000244|PDB:3RDE}.
HELIX 444 450 {ECO:0000244|PDB:3RDE}.
HELIX 460 483 {ECO:0000244|PDB:3RDE}.
HELIX 487 491 {ECO:0000244|PDB:3RDE}.
HELIX 494 505 {ECO:0000244|PDB:3RDE}.
TURN 506 509 {ECO:0000244|PDB:3RDE}.
HELIX 512 514 {ECO:0000244|PDB:3RDE}.
HELIX 523 537 {ECO:0000244|PDB:3RDE}.
HELIX 539 545 {ECO:0000244|PDB:3RDE}.
HELIX 548 551 {ECO:0000244|PDB:3RDE}.
STRAND 552 554 {ECO:0000244|PDB:3RDE}.
HELIX 555 557 {ECO:0000244|PDB:3RDE}.
STRAND 568 570 {ECO:0000244|PDB:3RDE}.
HELIX 574 580 {ECO:0000244|PDB:3RDE}.
HELIX 584 598 {ECO:0000244|PDB:3RDE}.
HELIX 618 643 {ECO:0000244|PDB:3RDE}.
STRAND 645 647 {ECO:0000244|PDB:3RDE}.
TURN 654 656 {ECO:0000244|PDB:3RDE}.
STRAND 657 660 {ECO:0000244|PDB:3RDE}.
SEQUENCE 663 AA; 75004 MW; 5E3864A7A3FDEF71 CRC64;
MGLYRVRVST GSSFYAGSQN QVQLWLVGQH GEAALGWCLR PARGKETEFS VDVSEYLGPL
LFVKLRKRHL LQDDAWFCNW ISVQGPGANG DEFRFPCYRW VEGDRILSLP EGTARTVVDD
PQGLFKKHRE EELAERRKLY RWGNWKDGLI LNIASTGIHD LPVDERFLED KRIDFEASLA
KGLADLAVKD SLNVLMSWNS LDSFNRIFWC GQSKLAERVR DSWKEDALFG YQFLNGTNPM
LLRHSVELPA RLKFPPGMEE LQAQLEKELQ GGTLFEADFS LLDGIKANVI LCSQQYLAVP
LVMLKLQPDG KLLPMVIQLQ LPHEGSPLPP LFLPTDPPMV WLLAKCWVRS SDFQLHELHS
HLLRGHLMAE VIAVATMRCL PSIHPIFKLL IPHFRYTMEI NVRARNGLVS DLGIFDQVVS
TGGGGHVELL RRAAALLTYS SFCPPDDLAD RGLLGVESSF YAQDALRLWE VISRYVEGIV
SLHYKTDESV KEDLELQAWC REFTEIGLLG AQDRGFPVSL QSKEQLCHFV TMCIFTCTGQ
HSSNHLGQLD WYSWVPNAPC TMRLPPPTTK DATLETVMAT LPNFHQASLQ MSITWQLGRC
QPTMVALGQH EEEYFSGPGP KAVLTKFREE LAALDKDIEV RNAKLALPYE YLRPSRVENS
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