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Seed linoleate 13S-lipoxygenase-1 (EC 1.13.11.12) (Lipoxygenase-1) (L-1)

 LOX1_SOYBN              Reviewed;         839 AA.
P08170;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
23-MAY-2018, entry version 166.
RecName: Full=Seed linoleate 13S-lipoxygenase-1;
EC=1.13.11.12 {ECO:0000269|PubMed:16157595, ECO:0000269|PubMed:2492826};
AltName: Full=Lipoxygenase-1;
Short=L-1;
Name=LOX1.1; Synonyms=LOX1;
Glycine max (Soybean) (Glycine hispida).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Glycine; Soja.
NCBI_TaxID=3847;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3112136;
Shibata D., Steczko J., Dixon J.E., Hermodson M., Yazdanparast R.,
Axelrod B.;
"Primary structure of soybean lipoxygenase-1.";
J. Biol. Chem. 262:10080-10085(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Bonminori; TISSUE=Cotyledon;
Fukazawa C., Masayoshi M., Chikafusa F.;
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 426-752.
AGRICOLA=IND87003970; DOI=10.1007/BF00020127;
Start W.G., Ma Y., Polacco J.C., Hildebrand D.F., Freyer G.A.,
Altschuler M.;
"Two soybean seed lipoxygenase nulls accumulate reduced levels of
lipoxygenase transcripts.";
Plant Mol. Biol. 7:11-23(1986).
[4]
SEQUENCE REVISION TO 479-482, AND MUTAGENESIS OF SOME HISTIDINE
RESIDUES.
PubMed=1567851; DOI=10.1021/bi00131a022;
Steczko J., Donoho G.P., Clemens J.C., Dixon J.E., Axelrod B.;
"Conserved histidine residues in soybean lipoxygenase: functional
consequences of their replacement.";
Biochemistry 31:4053-4057(1992).
[5]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SPECIFICITY.
PubMed=2492826; DOI=10.1016/0005-2760(89)90111-2;
Gardner H.W.;
"Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-
hydroperoxides from linoleic acid by a pH-dependent mechanism.";
Biochim. Biophys. Acta 1001:274-281(1989).
[6]
MUTAGENESIS OF SOME HISTIDINE RESIDUES.
PubMed=1497657; DOI=10.1016/0006-291X(92)90801-Q;
Steczko J., Axelrod B.;
"Identification of the iron-binding histidine residues in soybean
lipoxygenase L-1.";
Biochem. Biophys. Res. Commun. 186:686-689(1992).
[7]
COFACTOR.
PubMed=8518276; DOI=10.1021/bi00076a003;
Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B.;
"Crystallographic determination of the active site iron and its
ligands in soybean lipoxygenase L-1.";
Biochemistry 32:6320-6323(1993).
[8]
CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ALA-542, ENZYME KINETICS,
REACTION MECHANISM, AND EPR SPECTROSCOPY.
PubMed=16157595; DOI=10.1074/jbc.M504870200;
Coffa G., Imber A.N., Maguire B.C., Laxmikanthan G., Schneider C.,
Gaffney B.J., Brash A.R.;
"On the relationships of substrate orientation, hydrogen abstraction,
and product stereochemistry in single and double dioxygenations by
soybean lipoxygenase-1 and its Ala542Gly mutant.";
J. Biol. Chem. 280:38756-38766(2005).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS.
PubMed=8502991; DOI=10.1126/science.8502991;
Boyington J.C., Gaffney B.J., Amzel L.M.;
"The three-dimensional structure of an arachidonic acid 15-
lipoxygenase.";
Science 260:1482-1486(1993).
[10]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.
PubMed=8718858; DOI=10.1021/bi960576u;
Minor W., Steczko J., Stec B., Otwinowski Z., Bolin J.T., Walter R.,
Axelrod B.;
"Crystal structure of soybean lipoxygenase L-1 at 1.4-A resolution.";
Biochemistry 35:10687-10701(1996).
[11]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-495
AND GLN-697 IN COMPLEX WITH IRON IONS, AND MUTAGENESIS OF GLN-495 AND
GLN-697.
PubMed=11412104; DOI=10.1021/bi002893d;
Tomchick D.R., Phan P., Cymborowski M., Minor W., Holman T.R.;
"Structural and functional characterization of second-coordination
sphere mutants of soybean lipoxygenase-1.";
Biochemistry 40:7509-7517(2001).
-!- FUNCTION: Plant lipoxygenase may be involved in a number of
diverse aspects of plant physiology including growth and
development, pest resistance, and senescence or responses to
wounding. With linoleate as substrate, L-1 shows a preference for
carbon 13 as the site for hydroperoxidation (in contrast to L-2
and L-3, which utilize either carbon 9 or 13). At pH above 8.5,
only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is
produced, but as the pH decreases, the proportion of (9S)-
hydroperoxide increases linearly until at pH 6.0 it represents
about 25 % of the products. {ECO:0000269|PubMed:16157595}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E,13S)-13-
hydroperoxyoctadeca-9,11-dienoate. {ECO:0000269|PubMed:16157595,
ECO:0000269|PubMed:2492826}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,11E,13S,15Z)-13-
hydroperoxyoctadeca-9,11,15-trienoate.
{ECO:0000269|PubMed:16157595, ECO:0000269|PubMed:2492826}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00726,
ECO:0000269|PubMed:8518276};
Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
{ECO:0000255|PROSITE-ProRule:PRU00726,
ECO:0000269|PubMed:8518276};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Inactive below pH 6.0. {ECO:0000269|PubMed:2492826};
-!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11412104,
ECO:0000269|PubMed:8502991, ECO:0000269|PubMed:8718858}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: The hydroperoxide product serves to activate the
resting enzyme. The activation is accompanied by the oxidation of
Fe(2+)entadiene structure. L-1 prefers anionic substrate.
-!- MISCELLANEOUS: Soybean contains at least 4 distinct isoenzymes, L-
1, L-2, L-3a and L-3b in dry seeds, and at least two distinct
isozymes in the hypocotyl/radicle region of the seedling stem.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA47717.1; Type=Frameshift; Positions=663, 697; Evidence={ECO:0000305};
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EMBL; J02795; AAA33986.1; -; mRNA.
EMBL; X67304; CAA47717.1; ALT_FRAME; mRNA.
PIR; S25064; DASYL2.
RefSeq; NP_001236153.1; NM_001249224.1.
UniGene; Gma.947; -.
PDB; 1F8N; X-ray; 1.40 A; A=1-839.
PDB; 1FGM; X-ray; 1.90 A; A=1-839.
PDB; 1FGO; X-ray; 1.62 A; A=1-839.
PDB; 1FGQ; X-ray; 1.85 A; A=1-839.
PDB; 1FGR; X-ray; 1.60 A; A=1-839.
PDB; 1FGT; X-ray; 1.62 A; A=1-839.
PDB; 1Y4K; X-ray; 1.95 A; A=1-839.
PDB; 1YGE; X-ray; 1.40 A; A=1-839.
PDB; 2SBL; X-ray; 2.60 A; A/B=1-839.
PDB; 3BNB; X-ray; 1.45 A; A=1-839.
PDB; 3BNC; X-ray; 1.65 A; A=1-839.
PDB; 3BND; X-ray; 1.60 A; A=1-839.
PDB; 3BNE; X-ray; 1.40 A; A=1-839.
PDB; 3PZW; X-ray; 1.40 A; A=1-839.
PDB; 4WFO; X-ray; 1.14 A; A=1-839.
PDB; 4WHA; X-ray; 1.70 A; A=1-839.
PDB; 5EEO; X-ray; 2.10 A; A=1-839.
PDB; 5T5V; X-ray; 1.80 A; A/B=1-839.
PDB; 5TQN; X-ray; 1.80 A; A/B=1-839.
PDB; 5TQO; X-ray; 1.70 A; A/B=1-839.
PDB; 5TQP; X-ray; 1.70 A; A/B=1-839.
PDB; 5TR0; X-ray; 1.85 A; A/B=1-839.
PDBsum; 1F8N; -.
PDBsum; 1FGM; -.
PDBsum; 1FGO; -.
PDBsum; 1FGQ; -.
PDBsum; 1FGR; -.
PDBsum; 1FGT; -.
PDBsum; 1Y4K; -.
PDBsum; 1YGE; -.
PDBsum; 2SBL; -.
PDBsum; 3BNB; -.
PDBsum; 3BNC; -.
PDBsum; 3BND; -.
PDBsum; 3BNE; -.
PDBsum; 3PZW; -.
PDBsum; 4WFO; -.
PDBsum; 4WHA; -.
PDBsum; 5EEO; -.
PDBsum; 5T5V; -.
PDBsum; 5TQN; -.
PDBsum; 5TQO; -.
PDBsum; 5TQP; -.
PDBsum; 5TR0; -.
ProteinModelPortal; P08170; -.
SMR; P08170; -.
STRING; 3847.GLYMA13G42320.1; -.
BindingDB; P08170; -.
ChEMBL; CHEMBL4586; -.
SwissLipids; SLP:000001639; -.
GeneID; 547923; -.
KEGG; gmx:547923; -.
InParanoid; P08170; -.
KO; K15718; -.
SABIO-RK; P08170; -.
UniPathway; UPA00382; -.
EvolutionaryTrace; P08170; -.
PRO; PR:P08170; -.
Proteomes; UP000008827; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 4.10.372.10; -; 1.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR036226; LipOase_C_sf.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001246; LipOase_plant.
InterPro; IPR027433; Lipoxygenase_dom_3.
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; PR00468; PLTLPOXGNASE.
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; Complete proteome; Cytoplasm; Dioxygenase;
Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
Reference proteome.
CHAIN 1 839 Seed linoleate 13S-lipoxygenase-1.
/FTId=PRO_0000220717.
DOMAIN 16 145 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 148 839 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 499 499 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:8502991}.
METAL 504 504 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:8502991}.
METAL 690 690 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726,
ECO:0000269|PubMed:8502991}.
METAL 694 694 Iron; catalytic.
METAL 839 839 Iron; via carboxylate; catalytic.
MUTAGEN 494 494 H->Q: 37% of wild-type activity.
MUTAGEN 494 494 H->S: 8% of wild-type activity.
MUTAGEN 495 495 Q->A: Reduces catalytic activity.
{ECO:0000269|PubMed:11412104}.
MUTAGEN 495 495 Q->E: No effect on catalytic activity.
{ECO:0000269|PubMed:11412104}.
MUTAGEN 499 499 H->Q: Inactive.
MUTAGEN 504 504 H->Q,S: Inactive.
MUTAGEN 517 517 H->Q: 33% of wild-type activity.
MUTAGEN 522 522 H->Q: 1% of wild-type activity.
MUTAGEN 531 531 H->Q: 20% of wild-type activity.
MUTAGEN 542 542 A->G: Changes reaction profile to produce
almost equal amounts of 13S- and 9R-
hydroperoxyoctadecadienoate.
{ECO:0000269|PubMed:16157595}.
MUTAGEN 542 542 A->S: Little effect on reaction profile.
{ECO:0000269|PubMed:16157595}.
MUTAGEN 542 542 A->T,V: Complete loss of activity.
{ECO:0000269|PubMed:16157595}.
MUTAGEN 690 690 H->Q: Inactive.
MUTAGEN 697 697 Q->N,E: Reduces catalytic activity.
{ECO:0000269|PubMed:11412104}.
CONFLICT 426 427 AK -> RN (in Ref. 3). {ECO:0000305}.
CONFLICT 558 560 LPS -> AL (in Ref. 3). {ECO:0000305}.
CONFLICT 572 574 KNW -> EL (in Ref. 3). {ECO:0000305}.
CONFLICT 641 641 N -> P (in Ref. 3). {ECO:0000305}.
CONFLICT 741 748 KLPTLISL -> SCRLSLAV (in Ref. 3).
{ECO:0000305}.
STRAND 7 16 {ECO:0000244|PDB:4WFO}.
HELIX 17 19 {ECO:0000244|PDB:4WFO}.
HELIX 24 26 {ECO:0000244|PDB:1YGE}.
HELIX 32 35 {ECO:0000244|PDB:4WFO}.
STRAND 39 50 {ECO:0000244|PDB:4WFO}.
STRAND 56 58 {ECO:0000244|PDB:4WFO}.
STRAND 66 68 {ECO:0000244|PDB:4WFO}.
STRAND 79 86 {ECO:0000244|PDB:4WFO}.
HELIX 89 91 {ECO:0000244|PDB:4WFO}.
STRAND 94 101 {ECO:0000244|PDB:4WFO}.
STRAND 103 105 {ECO:0000244|PDB:4WFO}.
STRAND 107 114 {ECO:0000244|PDB:4WFO}.
HELIX 119 121 {ECO:0000244|PDB:4WFO}.
STRAND 123 131 {ECO:0000244|PDB:4WFO}.
HELIX 134 136 {ECO:0000244|PDB:4WFO}.
STRAND 141 144 {ECO:0000244|PDB:4WFO}.
HELIX 151 153 {ECO:0000244|PDB:4WFO}.
HELIX 156 158 {ECO:0000244|PDB:4WFO}.
HELIX 159 170 {ECO:0000244|PDB:4WFO}.
TURN 195 197 {ECO:0000244|PDB:4WFO}.
HELIX 199 201 {ECO:0000244|PDB:4WFO}.
STRAND 206 212 {ECO:0000244|PDB:4WFO}.
HELIX 242 244 {ECO:0000244|PDB:4WFO}.
HELIX 251 253 {ECO:0000244|PDB:4WFO}.
HELIX 255 257 {ECO:0000244|PDB:4WFO}.
HELIX 258 264 {ECO:0000244|PDB:4WFO}.
HELIX 266 275 {ECO:0000244|PDB:4WFO}.
HELIX 286 290 {ECO:0000244|PDB:4WFO}.
HELIX 291 293 {ECO:0000244|PDB:4WFO}.
HELIX 301 307 {ECO:0000244|PDB:4WFO}.
HELIX 313 316 {ECO:0000244|PDB:4WFO}.
STRAND 317 319 {ECO:0000244|PDB:1Y4K}.
STRAND 321 326 {ECO:0000244|PDB:4WFO}.
HELIX 331 333 {ECO:0000244|PDB:4WFO}.
HELIX 339 341 {ECO:0000244|PDB:4WFO}.
HELIX 343 352 {ECO:0000244|PDB:4WFO}.
STRAND 353 355 {ECO:0000244|PDB:4WFO}.
STRAND 364 366 {ECO:0000244|PDB:4WFO}.
HELIX 373 376 {ECO:0000244|PDB:4WFO}.
HELIX 385 387 {ECO:0000244|PDB:4WFO}.
HELIX 395 400 {ECO:0000244|PDB:4WFO}.
STRAND 404 408 {ECO:0000244|PDB:4WFO}.
HELIX 410 421 {ECO:0000244|PDB:4WFO}.
STRAND 430 437 {ECO:0000244|PDB:4WFO}.
STRAND 443 451 {ECO:0000244|PDB:4WFO}.
STRAND 456 458 {ECO:0000244|PDB:4WFO}.
STRAND 465 467 {ECO:0000244|PDB:4WFO}.
HELIX 473 496 {ECO:0000244|PDB:4WFO}.
HELIX 497 503 {ECO:0000244|PDB:4WFO}.
HELIX 504 517 {ECO:0000244|PDB:4WFO}.
HELIX 523 528 {ECO:0000244|PDB:4WFO}.
HELIX 529 532 {ECO:0000244|PDB:4WFO}.
HELIX 535 545 {ECO:0000244|PDB:4WFO}.
HELIX 552 556 {ECO:0000244|PDB:4WFO}.
HELIX 560 562 {ECO:0000244|PDB:4WFO}.
HELIX 563 571 {ECO:0000244|PDB:4WFO}.
HELIX 576 579 {ECO:0000244|PDB:4WFO}.
HELIX 581 587 {ECO:0000244|PDB:4WFO}.
STRAND 590 593 {ECO:0000244|PDB:4WFO}.
STRAND 600 605 {ECO:0000244|PDB:4WFO}.
HELIX 609 628 {ECO:0000244|PDB:4WFO}.
HELIX 629 631 {ECO:0000244|PDB:4WFO}.
HELIX 636 640 {ECO:0000244|PDB:4WFO}.
HELIX 643 654 {ECO:0000244|PDB:4WFO}.
TURN 655 657 {ECO:0000244|PDB:4WFO}.
HELIX 658 660 {ECO:0000244|PDB:4WFO}.
STRAND 669 671 {ECO:0000244|PDB:1YGE}.
HELIX 672 686 {ECO:0000244|PDB:4WFO}.
HELIX 688 694 {ECO:0000244|PDB:4WFO}.
HELIX 697 701 {ECO:0000244|PDB:4WFO}.
TURN 704 706 {ECO:0000244|PDB:4WFO}.
STRAND 718 720 {ECO:0000244|PDB:5TR0}.
HELIX 721 728 {ECO:0000244|PDB:4WFO}.
HELIX 730 737 {ECO:0000244|PDB:4WFO}.
HELIX 741 754 {ECO:0000244|PDB:4WFO}.
HELIX 776 801 {ECO:0000244|PDB:4WFO}.
HELIX 803 805 {ECO:0000244|PDB:4WFO}.
HELIX 806 809 {ECO:0000244|PDB:4WFO}.
TURN 810 814 {ECO:0000244|PDB:4WFO}.
STRAND 826 828 {ECO:0000244|PDB:4WFO}.
STRAND 834 836 {ECO:0000244|PDB:4WFO}.
SEQUENCE 839 AA; 94369 MW; 1586250ACD3E34A4 CRC64;
MFSAGHKIKG TVVLMPKNEL EVNPDGSAVD NLNAFLGRSV SLQLISATKA DAHGKGKVGK
DTFLEGINTS LPTLGAGESA FNIHFEWDGS MGIPGAFYIK NYMQVEFFLK SLTLEAISNQ
GTIRFVCNSW VYNTKLYKSV RIFFANHTYV PSETPAPLVS YREEELKSLR GNGTGERKEY
DRIYDYDVYN DLGNPDKSEK LARPVLGGSS TFPYPRRGRT GRGPTVTDPN TEKQGEVFYV
PRDENLGHLK SKDALEIGTK SLSQIVQPAF ESAFDLKSTP IEFHSFQDVH DLYEGGIKLP
RDVISTIIPL PVIKELYRTD GQHILKFPQP HVVQVSQSAW MTDEEFAREM IAGVNPCVIR
GLEEFPPKSN LDPAIYGDQS SKITADSLDL DGYTMDEALG SRRLFMLDYH DIFMPYVRQI
NQLNSAKTYA TRTILFLRED GTLKPVAIEL SLPHSAGDLS AAVSQVVLPA KEGVESTIWL
LAKAYVIVND SCYHQLMSHW LNTHAAMEPF VIATHRHLSV LHPIYKLLTP HYRNNMNINA
LARQSLINAN GIIETTFLPS KYSVEMSSAV YKNWVFTDQA LPADLIKRGV AIKDPSTPHG
VRLLIEDYPY AADGLEIWAA IKTWVQEYVP LYYARDDDVK NDSELQHWWK EAVEKGHGDL
KDKPWWPKLQ TLEDLVEVCL IIIWIASALH AAVNFGQYPY GGLIMNRPTA SRRLLPEKGT
PEYEEMINNH EKAYLRTITS KLPTLISLSV IEILSTHASD EVYLGQRDNP HWTSDSKALQ
AFQKFGNKLK EIEEKLVRRN NDPSLQGNRL GPVQLPYTLL YPSSEEGLTF RGIPNSISI


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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
U1965m CLIA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 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
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
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
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
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
E1965b ELISA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
U1965b CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
U1355r CLIA 5-lipoxygenase,5-LO,Alox5,Arachidonate 5-lipoxygenase,Rat,Rattus norvegicus 96T


 

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