15 Lipoxygenase 2 Protein, Human (sf9)

15-Lipoxygenase 2 (15-LOX2) is a non-heme iron-containing dioxygenase with a crucial role in catalyzing stereo-specific peroxidation of both free and esterified polyunsaturated fatty acids (PUFAs), generating a diverse array of bioactive lipid mediators. This enzyme exhibits peroxidase activity on arachidonate, producing (15S)-hydroperoxyeicosatetraenoate/(15S)-HPETE, and on linoleate, generating 13-hydroperoxyoctadecadienoate/13-HPODE. Moreover, it oxygenates arachidonyl derivatives such as 2-arachidonoylglycerol (2-AG), leading to the production of 15-hydroxyeicosatetraenoyl glycerol (15-HETE-G), which acts as a peroxisome proliferator-activated receptor alpha agonist. 15-LOX2 efficiently class-switches pro-inflammatory mediators into anti-inflammatory intermediates and participates in the sequential oxidations of docosahexaenoate (DHA) to generate specialized pro-resolving mediators (SPMs) like resolvin D5. Besides its role in lipid metabolism, 15-LOX2 may influence cell cycle progression, cell proliferation, cytokine secretion by macrophages, and macrophage differentiation into proatherogenic foam cells. Importantly, it does not convert arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE, highlighting its substrate specificity.