15 Lipoxygenase 2 Protein, Human (sf9, His-GST)

15-lipoxygenase 2 (15-LOX2) is a nonheme iron-containing dioxygenase essential for the peroxidation of polyunsaturated fatty acids (PUFA). It exhibits peroxidase activity towards arachidonic acid and linoleic acid, producing bioactive lipid mediators. 15 Lipoxygenase 2 Protein, Human (sf9, His-GST) is the recombinant human-derived 15 Lipoxygenase 2 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of 15 Lipoxygenase 2 Protein, Human (sf9, His-GST) is 676 a.a., with molecular weight of ~93 kDa.

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.

Human

Sf9 insect cells

N-His;N-GST

O15296 (M1-I676)

247  [NCBI]

Approximately 93 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.