Recombinant Human ALOX12 protein

Specification
Description Recombinant protein from the full-length sequence of Homo sapiens arachidonate 12-lipoxygenase, 12S type (ALOX12) (NM_000697).
Organism Homo sapiens (Human)
Expression Host Human Cells
Tag Info His or DYKDDDDK. Please contact us if you need further information or require specific designed tag.
Purity Greater than 90% by SDS-PAGE gel
Uniprot ID P18054
Entry Name LOX12_HUMAN
Gene Names ALOX12 12LO LOG12
Alternative Gene Names 12LO LOG12
Alternative Protein Names Polyunsaturated fatty acid lipoxygenase ALOX12 (EC 1.13.11.-) (Arachidonate (12S)-lipoxygenase) (12S-LOX) (12S-lipoxygenase) (EC 1.13.11.31) (Arachidonate (15S)-lipoxygenase) (EC 1.13.11.33) (Linoleate (13S)-lipoxygenase) (Lipoxin synthase 12-LO) (EC 3.3.2.-) (Platelet-type lipoxygenase 12)
Application Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only!
Buffer Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives
Endotoxin Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg)
Length 663
Molecular Weight(Da) 75694
Protein Sequence (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.)
MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI
Background
Function FUNCTION: Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:17493578, PubMed:1851637, PubMed:8319693, PubMed:8500694, PubMed:18311922, PubMed:32404334). Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE (PubMed:17493578, PubMed:22984144, PubMed:24282679, PubMed:8319693, PubMed:8500694). Through the production of bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation (PubMed:8319693, PubMed:8500694). It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA (PubMed:23504711). Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively downregulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334). An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites (PubMed:8250832). Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)-hydroperoxyoctadecadienoate/ (13S-HPODE) (By similarity). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic (PubMed:9751607, PubMed:16638750, PubMed:22237009). Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells (PubMed:23578768). {ECO:0000250|UniProtKB:P39655, ECO:0000269|PubMed:16638750, ECO:0000269|PubMed:17493578, ECO:0000269|PubMed:18311922, ECO:0000269|PubMed:1851637, ECO:0000269|PubMed:22237009, ECO:0000269|PubMed:22984144, ECO:0000269|PubMed:23504711, ECO:0000269|PubMed:23578768, ECO:0000269|PubMed:24282679, ECO:0000269|PubMed:32404334, ECO:0000269|PubMed:8250832, ECO:0000269|PubMed:8319693, ECO:0000269|PubMed:8500694, ECO:0000269|PubMed:9751607}.
Pathway Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.
Protein Families Lipoxygenase family
Tissue Specificity Expressed in vascular smooth muscle cells. {ECO:0000269|PubMed:23578768}.
QC Data
Note Please contact us for QC Data
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EB-EPE8011895

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