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Cyclooxygenase 1 (COX-1) is a bifunctional enzyme that exhibits both COX and peroxidase activities.1,2 It is composed of an N-terminal signal peptide, an EGF-like domain, a membrane binding domain, a catalytic domain, and a C-terminal tail.3 COX-1 is constitutively expressed in the gastrointestinal tract, kidney, spleen, liver, and lung and localizes to the endoplasmic reticulum.4,5 The COX component converts arachidonic acid (Item Nos. 90010 | 90010.1 | 10006607) to a hydroperoxyl endoperoxide prostaglandin G2 (PGG2; Item No. 17010) and the peroxidase component reduces the endoperoxide to the corresponding alcohol PGH2 (Item No. 17020), the precursor of PGs, thromboxanes, and prostacyclins.1,2 COX-1 is the target of many non-steroidal anti-inflammatory drugs (NSAIDs) and is responsible for the undesirable gastrointestinal and renal side effects, such as ulcer formation and reductions in the glomerular filtration rate, respectively.6,7 Cayman’s COX-1 (ovine) protein can be used for enzyme activity assays.
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From Vietnamese plants to a biflavonoid that relieves inflammation by triggering the lipid mediator class switch to resolution. Acta Pharm. Sin. B. 11(6), 1629-1647 (2021).
Differential cyclooxygenase expression levels and survival associations in type I and type II ovarian tumors. J. Ovarian Res. 11(17), (2018).
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Inhibition by tectorigenin and tectoridin of prostaglandin E2 production and cyclooxygenase-