GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.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.
28-MAR-2018, entry version 142.
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 https://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 droplet; 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.
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;
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 :
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
Pathways :
WP668: Octadecanoid Pathway
WP1000: Arachidonate Epoxygenase Epoxide Hydrolase
WP1116: Arachidonate Epoxygenase Epoxide Hydrolase
WP1250: Arachidonate Epoxygenase Epoxide Hydrolase
WP1285: Arachidonate Epoxygenase Epoxide Hydrolase
WP678: Arachidonate Epoxygenase / Epoxide Hydrolase
WP882: Arachidonate Epoxygenase Epoxide Hydrolase
WP1011: T Cell Receptor Signaling Pathway
WP1017: Type II interferon signaling (IFNG)
WP1025: B Cell Receptor Signaling Pathway
WP1043: Calcium Regulation in the Cardiac Cell
WP1069: Integrin-mediated cell adhesion
WP1078: G1 to S cell cycle control
WP1083: Cell cycle
WP1130: T Cell Receptor Signaling Pathway
WP1136: Type II interferon signaling (IFNG)
WP1144: B Cell Receptor Signaling Pathway
WP1159: Calcium Regulation in the Cardiac Cell
WP1185: Integrin-mediated cell adhesion
WP1195: G1 to S cell cycle control
WP1200: Cell cycle
WP1253: Type II interferon signaling (IFNG)
WP1289: Type II interferon signaling (IFNG)
WP133: Fatty Acid Omega Oxidation
WP1345: T Cell Receptor Signaling Pathway
Related Genes :
[ALOX15] 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)
[ALOX15 LOG15] Arachidonate 15-lipoxygenase (15-LOX) (15-LOX-1) (EC 1.13.11.33) (12/15-lipoxygenase) (Arachidonate 12-lipoxygenase, leukocyte-type) (12-LOX) (EC 1.13.11.31) (Arachidonate omega-6 lipoxygenase)
[Alox15 Alox12l] 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)
[ALOX15] 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)
[ALOX15] 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)
[Alox15 Alox12l] 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)
[ALOX15] 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)
[Alox8 Alox15b] Arachidonate 8S-lipoxygenase (8-LOX) (8S-LOX) (EC 1.13.11.-) (15-lipoxygenase 2) (15-LOX-2) (Arachidonate 15-lipoxygenase B) (15-LOX-B)
[ALOX15B] Arachidonate 15-lipoxygenase B (15-LOX-B) (EC 1.13.11.33) (15-lipoxygenase 2) (15-LOX-2) (Arachidonate 15-lipoxygenase type II) (Linoleate 13-lipoxygenase 15-LOb) (EC 1.13.11.-)
[Alox15b] Arachidonate 15-lipoxygenase B (15-LOX-B) (EC 1.13.11.33) (15-lipoxygenase 2) (15-LOX-2) (Arachidonate 15-lipoxygenase type II) (Linoleate 13-lipoxygenase 15-LOb) (EC 1.13.11.-)
[ALOX12 12LO LOG12] Arachidonate 12-lipoxygenase, 12S-type (12S-LOX) (12S-lipoxygenase) (EC 1.13.11.31) (Lipoxin synthase 12-LO) (EC 3.3.2.-) (Platelet-type lipoxygenase 12)
[] Allene oxide synthase-lipoxygenase protein [Includes: Allene oxide synthase (EC 4.2.1.92) (Hydroperoxidehydrase); Arachidonate 8-lipoxygenase (EC 1.13.11.40)]
[ALOX5 LOG5] Arachidonate 5-lipoxygenase (5-LO) (5-lipoxygenase) (EC 1.13.11.34)
[Alox12 Alox12p] Arachidonate 12-lipoxygenase, 12S-type (12S-LOX) (12S-lipoxygenase) (EC 1.13.11.31) (Lipoxin synthase 12-LO) (EC 3.3.2.-) (Platelet-type lipoxygenase 12) (P-12LO)
[Alox5] Arachidonate 5-lipoxygenase (5-LO) (5-lipoxygenase) (EC 1.13.11.34)
[Alox5] Arachidonate 5-lipoxygenase (5-LO) (5-lipoxygenase) (EC 1.13.11.34)
[Alox12b Aloxe2] Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12) (Epidermis-type lipoxygenase 2) (e-LOX 2)
[Alox12] Arachidonate 12-lipoxygenase, 12S-type (12S-LOX) (12S-lipoxygenase) (EC 1.13.11.31) (Lipoxin synthase 12-LO) (EC 3.3.2.-) (Platelet-type lipoxygenase 12)
[ALOX12B] Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12)
[Alox5ap Flap] Arachidonate 5-lipoxygenase-activating protein (FLAP) (MK-886-binding protein)
[ALOX5AP FLAP] Arachidonate 5-lipoxygenase-activating protein (FLAP) (MK-886-binding protein)
[Alox12b] Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12)
[Alox5ap Flap] Arachidonate 5-lipoxygenase-activating protein (FLAP) (MK-886-binding protein)
[Alox12e Alox12-ps2 Aloxe] Arachidonate 12-lipoxygenase, epidermal-type (12-LOX) (EC 1.13.11.31)
[ALOX5] Arachidonate 5-lipoxygenase (5-LO) (5-lipoxygenase) (EC 1.13.11.34)
[cyp102A1 cyp102 BG04_163] Bifunctional cytochrome P450/NADPH--P450 reductase (Cytochrome P450(BM-3)) (Cytochrome P450BM-3) (Fatty acid monooxygenase) (Flavocytochrome P450 BM3) [Includes: Cytochrome P450 102A1 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[Alox12e] Arachidonate 12-lipoxygenase, epidermal-type (12-LOX) (EC 1.13.11.31)
[loxA PA1169] Arachidonate 15-lipoxygenase (15-LOX) (EC 1.13.11.33)
[Alox15 mCG_21185] Arachidonate 15-lipoxygenase
[PTGS2 COX2] 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)
Bibliography :
No related Items
Enter catalog number :
Favorites Pages:
No Favorits