15-Lipoxygenase-2 (human, recombinant)

Two types of 15-lipoxygenase (15-LO) have been discovered and characterized, both of which metabolize arachidonic acid (AA) to produce 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE). 15-LO-1 oxygenates AA at both C-15 and C-12, whereas 15-LO-2 exclusively oxygenates C-15 of AA. Human 15-LO-2 has a molecular mass of approximately 76 kDa and exhibits approximately 40% identity to the reticulocyte 15-LO-1. Expression of 15-LO-2 appears to be restricted to prostate, lung, skin, and cornea and may play a role in the normal development of these tissues. The protein levels and enzymatic activity of 15-LO-2 are both down-regulated in prostate cancer compared with normal and benign prostate tissues, implicating a possible protective role for 15-LO-2 against tumor formation. Cayman's 15-LO-2 (human, recombinant) is expressed and purified from E. coli. The purity was determined using gel electrophoresis followed by coomassie staining. 15-LO-2 specific activity was established using arachidonic acid as the substrate and monitoring diene formation by measuring absorbance 236 nm.Synonyms: 15-LOX-2, 15-LO-2. Purity: >85% estimated by SDS-PAGE. Source: Active human recombinant C-terminal His-tagged protein expressed in E. coli. MW: 76 kDa. Formulation: (Request formulation change), PBS, pH 7.5, with 1 mM DTT, 20% glycerol. UniProt Accession #: O15296.