SRP0410
ALOX15 active human
recombinant, expressed in baculovirus infected Sf9 cells, ≥60% (SDS-PAGE)
Synonym(s):
15LOX-1, arachidonate 15-lipoxygenase
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
Recommended Products
biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
Assay
≥60% (SDS-PAGE)
form
aqueous solution
mol wt
75 kDa
packaging
pkg of 20 μg
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... ALOX15(246)
General description
The gene ALOX15 (arachidonate 15-lipoxygenase) is mapped to human chromosome 17p13. It is mainly present in the epithelial cells in the upper airways, reticulocytes, eosinophils and macrophages. ALOX15 belongs to the dioxygenases family. It is an IL-4 (interleukin 4)/IL-13 target gene.
ALOX-15, also known as 15LOX-1, ω-6 lipoxygenase, or arachidonate 15-lipoxygenase (GenBank Accession No. NM_001140) amino acids 2- 662 (end) with N-terminal FLAG-tag, MW = 75kDa, expressed in Sf9 insect cells via a Baculovirus expression system.
ALOX-15, also known as 15LOX-1, ω-6 lipoxygenase, or arachidonate 15-lipoxygenase (GenBank Accession No. NM_001140) amino acids 2- 662 (end) with N-terminal FLAG-tag, MW = 75kDa, expressed in Sf9 insect cells via a Baculovirus expression system.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
ALOX15 (arachidonate 15-lipoxygenase) is involved in homeostatic as well as pathological responses. ALOX15 is responsible for the oxidation of unsaturated fatty acids (at the 15 position) to active hydroperoxy and epoxy metabolites. It is also responsible for the conversion of linoleic acid to anti-tumor 13-S-hydroxyoctadecadienoic acid. ALOX15 is required for IL-4 (interleukin-4)/IL-13-mediated macrophage polarization. In mice, it is a negative regulator of bone mineral density. It is also involved in fatty acid metabolism. It controls MAPK (mitogen activated protein kinase) signaling in human airway epithelial cells using phosphatidylethanolamine-binding protein.
Physical form
Formulated in Tris-Buffered Saline (TBS), pH 7.4, containing 1 mM Fe(NH4)2(SO4)2.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Prostaglandins, leukotrienes, and essential fatty acids, 74(4), 235-245 (2006-03-25)
15-lipoxygenase (15-LOX) belongs to the structurally and functionally related nonheme iron dioxygenases family. It has two isoforms, type-1 (leukocyte type) and type-2 (epidermis type) and converts arachidonic acid to eicosanoids including the anti-cancer 13-HODE. In the current study, we investigate
12/15 Lipoxygenase regulation of colorectal tumorigenesis is determined by the relative tumor levels of its metabolite 12-HETE and 13-HODE in animal models.
Oncotarget, 6, 2879-2879 (2015)
Polymorphisms in inflammation associated genes ALOX15 and IL-6 are associated with bone properties in young women and fracture in elderly.
Bone, 79, 105-105 (2015)
Biochemical and biophysical research communications, 157(2), 457-464 (1988-12-15)
A full-length cDNA encoding 15-lipoxygenase has been isolated from a human reticulocyte cDNA library. The predicted primary structure of the enzyme exhibits a sequence similarity of 61% and 45% with human 5-lipoxygenase and the soybean lipoxygenase isoenzyme I, respectively. When
15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells.
Proceedings of the National Academy of Sciences of the USA, 108, 14246-14246 (2011)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service