ALOX15B (aa 161_179)
- Known as:
- ALOX15B (aa 161_179)
- Catalog number:
- AP08226PU-N
- Product Quantity:
- 50 µg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- ALOX15B ( 161_179)
Related genes to: ALOX15B (aa 161_179)
- 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: ALOX15B (aa 161_179)
1,3_Di Methyl_2,4_Di Nitro Benzene 1,3_Di Methyl_2,4_Di Nit161
179
1H-indole-5-carbaldehyde, CAS Nr: 1196-69-6200ul Yellow Tip, Sterile200ul Yellow Tip, Sterile Sequenom Specials26S Proteasome Clone 'p32(26S-161) antibody Isotype IgG1 Host Mouse26S Proteasome (p32 subunit) Clone 'p32(26S-161) antibody Isotype IgG1 Host Mouse5a_Androstane_3a, 17b_diol Glucuronide (3a_Diol G)8-Strip Tubes, Clear 0.2ml, Ultra Thin Wall8-well PCR Strip Tubes, Clear8-well PCR Strip Tubes, Clear Ultra Thin Wall8-well PCR Strip Tubes, Clear Ultra Thin Wall8-well PCR Strip Tubes, Clear Ultra Thin Wall8_well PCR Tubes, Clear Ultra Thin Wall Related articles to: ALOX15B (aa 161_179)
- 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 - Papillary thyroid carcinoma (PTC) is the most common type of primary endocrine malignancy. The tumor immune microenvironment (TIME) and genetic alterations play crucial roles in the progression of PTC. With the advance in research, there has been a heightened focus on re-evaluating molecular targeted therapies and identifying novel targets through molecular biology-based approaches. This study aimed to identify robust prognostic biomarkers and to construct a reliable risk model for patients with PTC by integrating multiomics data. - Source: PubMed
Publication date: 2026/06/26
Xu NizhenShi ZhengZheng MingjieZhang DeguangHe QiqiZhu ChuZhang ZhenleiHe GaofeiChu JunjieJiang JinxiLu XiaoxiaoCai Xiujun - 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 - Metabolic dysfunction-associated steatotic liver disease (MASLD) is defined by aberrant hepatic lipid accumulation, yet the regulatory mechanisms underlying this process remain incompletely understood. Although epitranscriptomic modifications have emerged as key regulators of hepatic lipid homeostasis, the role of N-methylguanosine (mG) modification in hepatic steatosis remains unclear. - Source: PubMed
Publication date: 2026/06/27
Li LinghuanSun YuanhaiLi LingqinZheng WanfangBian JianingLi Hanbing