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Cyclooxygenase 2 (COX-2) is a bifunctional enzyme that exhibits both COX and peroxidase activities and catalyzes the first step in the biosynthesis of prostaglandins, thromboxanes, and prostacyclins.1,2 The COX component converts arachidonic acid to the hydroperoxy endoperoxide prostaglandin G2 (PGG2; Item No. 17010), and the peroxidase component reduces the endoperoxide to the corresponding alcohol PGH2 (Item No. 17020). COX-2 expression is induced by a variety of stimuli, including phorbol esters, LPS, and cytokines and is responsible for the biosynthesis of PGs under acute inflammatory conditions.3 Thus, COX-2 has been the focus of attention for the nonsteroidal anti-inflammatory drug (NSAID) development. Cayman's COX-2 (human, recombinant) contains an N-terminal hexahistidine tag and an alanine substituted for asparagine at position 580 (COX-2N580A) that prevents glycosylation at position 580 and decreases enzyme degradation in cells.4
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1. Isolation and properties of intermediates in prostaglandin biosynthesis. Biochim. Biophys. Acta 326(3), 448-461 (1973).
2. Detection and isolation of an endoperoxide intermediate in prostaglandin biosynthesis. Proc. Natl. Acad. Sci. USA 70(3), 899-903 (1973).
3. Structural and functional basis of cyclooxygenase inhibition. J. Med. Chem. 50(7), 1425-1441 (2007).
4. Glycosylation regulates turnover of cyclooxygenase-
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Characterisation of (R)-
Inhibition of endocannabinoid metabolism by the metabolites of ibuprofen and flurbiprofen. PLoS One 9(7), e103589 (2014).
Discovery of a novel dual fungal CYP51/human 5-