COX-1 (ovine) Polyclonal Antiserum

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) Polyclonal Antiserum can be used for Western blot (WB). The antibody recognizes COX-1 at 70 kDa from human, porcine, bovine endothelial, and ovine seminal vesicle samples.

WARNING This product is not for human or veterinary use.

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2. Hamberg, M., and Samuelsson, B. Detection and isolation of an endoperoxide intermediate in prostaglandin biosynthesis. Proc. Natl. Acad. Sci. USA 70(3), 899-903 (1973).

3. Smith, W.L., and DeWitt, D.L. Prostaglandin endoperoxide H synthases-1 and -2. Adv. Immunol. 62, 167-215 (1995).

4. Seibert, K., Zhang, Y., Leahy, K., et al. Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain. Proc. Natl. Acad. Sci. USA 91(25), 12013-12017 (1994).

5. Morita, I., Schindler, M., Regier, M.K., et al. Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2. The Journal of Biological Chemisty 270(18), 10902-10908 (1995).

6. Gierse, J.K., Hauser, S.D., Creely, D.P., et al. Expression and selective inhibition of the constitutive and inducible forms of human cyclo-oxygenase. Biochem. J. 305(Pt. 2), 379-484 (1995).

7. Frölich, J.C. A classification of NSAIDs according to the relative inhibition of cyclooxygenase isoenzymes. Trends Pharmacol. Sci. 18(1), 30-34 (1997).

Sun, Y., Jia, Z., Liu, G., et al. PPARγ agonist rosiglitazone suppresses renal mPGES-1/PGE₂ pathway in db/db mice. PPAR Res. 2013:e612971, (2013).

Nantel, F., Meadows, E., Denis, D., et al. Immunolocalization of cyclooxygenase-2 in the macula densa of human elderly. FEBS Lett. 457(3), 475-477 (1999).