ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus
- Known as:
- Enzyme-linked immunosorbent assay test reagent 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase classification II,Rat,Rattus norvegicus
- Catalog number:
- E1356r
- Product Quantity:
- 96T
- Category:
- -
- Supplier:
- EIAab
- Gene target:
- ELISA kit 15-lipoxygenase 2 15-LOX-2 15-LOX- Alox15b Arachidonate type Rat Rattus norvegicus
Related genes to: ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus
- Gene:
- ALOX15B NIH gene
- Name:
- arachidonate 15-lipoxygenase type B
- Previous symbol:
- -
- Synonyms:
- 15-LOX-2
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-22
- Date modifiied:
- 2019-01-18
Related products to: ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus
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- Mammalian arachidonic acid lipoxygenases (ALOXs) are non-heme iron-containing enzymes that oxygenate polyunsaturated fatty acids (PUFAs) with at least two isolated double bonds to hydroperoxy derivatives. The patho-physiological roles of these enzymes in inflammatory, hyperproliferative, and neurological diseases have made them promising targets for pharmacological interventions. Unfortunately, the expression levels of ALOX isoforms in mammalian cells are very low, which makes functional characterization of native enzymes and the development of isoform-specific inhibitors challenging. - Source: PubMed
Publication date: 2026/08/21
Aksenov VladislavKurchatova Angelina VGolovanov AlexeyUlasenko VeronikaZubkova OlgaZhuravlev AlexanderMakishvili EkaterinaKushlinskii Nikolay EKuhn HartmutIvanov Igor - Octyl (-(5-(1-indol-2-yl)-2-methoxyphenyl)sulfamoyl)carbamate has previously been characterized as substrate-specific inhibitor of the linoleic acid oxygenase activity of mammalian ALOX15 orthologs. Here we aimed at optimizing the inhibitory properties of this compound by three different chemical modifications: (i) replacement of the indole core by a phenylpyrrole; (ii) introduction of hydrophilic residues into the aliphatic hydrocarbon chain of the lead compound or by replacing this building block by a triethylene glycol moiety; (iii) replacement of the sulfamoylcarbamate group by a sulfonamide. The inhibitory potencies of the modified compounds for pure rabbit ALOX15 were quantified by in vitro inhibitory assays, and our data indicate that the replacement of the rigid indole core induced a partial loss in the inhibitor's potency. The introduction of a hydrophilic group into the aliphatic hydrocarbon chain or its replacement by a triethylene glycol moiety improved the solubility of the compound in aqueous solution, but reduced the inhibitor potency by more than one order of magnitude. Finally, the replacement of the sulfamoylcarbamate moiety by sulfonamide improved the substrate selectivity of the inhibitor for rabbit and human ALOX15. The new compounds were highly potent for human and rabbit ALOX15, but did not inhibit human ALOX15B and were less effective for mouse Alox15 (ortholog specificity). - Source: PubMed
Publication date: 2026/07/22
Gavrilyuk ViktorAksenov VladislavPetrov KirillKurchatova Angelina VBortnevskij DmitriyZhuravlev AlexanderGolovanov AlexeyKuhn HartmutIvanov Igor - Pancreatic cancer remains a devastating disease with limited therapeutic options. Accumulating evidence shows that cancer-associated fibroblasts (CAFs) and tumor-associated macrophages, the predominant cells in the pancreatic cancer (PDAC) tumor microenvironment, hinder antitumor immunity. However, the role of extracellular vesicles (EVs) in such a process is poorly understood. In this study, using human bone marrow-derived monocytes and PDAC tumor cells, we showed that tumor cell-derived EVs (TC-EVs) induced monocyte differentiation toward M2-like, immunosuppressive, CD200R+PD-L1+HLA-DRlo macrophages that express ALOX15B, that we identify as an independent PDAC poor-prognosis biomarker using a human PDAC metacohort. We also demonstrated that TC-EVs reprogrammed human primary PDAC CAFs, causing a fibronectin network reorganization associated with changes in extracellular matrix (ECM) composition, including alterations of WNT pathway elements such as secreted frizzled related protein-1 (SFRP1) enrichment. We also revealed that monocytes cultured on SFRP1-enriched ECM differentiated into M2-like, immunosuppressive macrophages. Last, we demonstrated that both directly and indirectly TC-EV- or SFRP1-enriched ECM-driven differentiated macrophages hindered T cell activation and subsequent antitumor activity. Our findings highlight potentially novel dual mechanisms of TC-EV-mediated crosstalk, involving ALOX15B+ macrophages and SFRP1+ CAFs, that simultaneously contribute to foster the immunosuppressive ecosystem of PDAC. - Source: PubMed
Publication date: 2026/07/02
Hussain ZainabMontenegro ClaudioRovera ChristopherBelghoula DjamilaTubiana Sarah SimhaFinetti PascalLohmann EugenieRodrigues MagdaBertran ThomasBidaut GhislainIsnardon DanielVasseur SophieBertucci FrancoisAudebert StephaneCamoin LucRego MoacyrTomasini Richard - Arachidonic acid lipoxygenases (ALOX-isoforms) have been implicated in cell differentiation and in the pathogenesis of various diseases. Human ALOX-isoforms prefer free polyunsaturated fatty acids as substrate but some of them are also capable of oxygenating complex ester lipids. Here we compared the reactivity of mammalian ALOX isoforms with complex lipid structures, explored the chemistry of the oxygenation products and characterized the structure of the enzyme-substrate complexes. We found that human and mouse ALOX15 orthologs as well as human ALOX15B are capable of oxidizing complex substates in the absence of adapter proteins and that the patterns of oxygenation products were similar to those of free fatty acid oxygenation. In contrast, the corresponding activities of mouse Alox15b and human ALOX12 were limited. Specific lipoxygenase products were also detected in the plasma lipids of mice with modified ALOX15 gene suggesting the in vivo activity of the enzyme on complex ester lipid substrates. - Source: PubMed
Publication date: 2026/06/08
Chen XinSträtker Sarah MelissaParvez SahanawazVabulas Ramunas MartinBochert AstridRothe MichaelHolzhütter Hermann-GeorgAparoy PolamarasettyKuhn Hartmut - Lipoxygenases (arachidonic acid lipoxygenase [ALOX]) are non-heme iron-containing dioxygenases that catalyze the oxygenation of polyenoic fatty acid-containing lipids to their corresponding hydroperoxy derivatives. These enzymes are widely distributed in highly developed plants and animals. In bacteria, they rarely occur, but they have not been detected in archaea and viruses. The human genome involves six functional ALOX genes (ALOX15, ALOX15B, ALOX12, ALOX12B, ALOXE3, and ALOX5) encoding for six different isoenzymes. The mouse genome carries an orthologous gene for each human ALOX gene, but in addition, an Aloxe12 gene has been identified in this species. The application of isoenzyme-specific loss-of-function strategies suggested that the coding multiplicity may not be interpreted as a sign of functional redundancy. In fact, the different isoenzymes apparently fulfill different biological functions. Mammalian ALOX15 orthologs are allosteric enzymes, but the molecular basis for their allosteric properties remains controversial. In fact, two alternative hypotheses (the presence of allosteric binding sites at enzyme monomers versus ALOX15 dimers consist of an allosteric and a catalytic monomer) have been introduced, and this review is aimed at critically evaluating the pros and cons of these two mechanistic scenarios. - Source: PubMed
Publication date: 2026/02/05
Yang JiaxingBorchert AstridKuhn Hartmut