Antigen: ovine COX-1 amino acids 272-282 (LMHYPRGIPPQ) · Host: rabbit · Application(s): WB, IHC, and ICC · COX-1 catalyzes the first step in the biosynthesis or prostaglandins, thromboxanes, and prostacyclins: the conversion of arachidonic acid to prostaglandin H₂. COX-1 is constitiutively expressed in almost all animal tissues and is involved in the homeostatic role of eicosanoids.^1,2 COX-1 is a 70 kDa protein which has been cloned from a variety of species including human, mouse, rat, and sheep.^3,4,5,6

1 Smith, W.L., and Marnett, L.J. Prostaglandin endoperoxide synthase: Structure and catalysis. Biochim Biophys Acta 1083 1-17 (1991).

2 Marnett, L.J., and Maddipati, K.R. Prostaglandin H synthase. 293-334 (1991).

3 DeWitt, D.L., and Smith, W.L. Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence. Proc Natl Acad Sci USA 85 1412-1416 (1988).

4 Funk, C.D., Funk, L.B., Kennedy, M.E., et al. Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment. FASEB J 5 2304-2312 (1991).

5 DeWitt, D.L., El-Harith, E.A., Kraemer, S.A., et al. The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases. J Biol Chem 265 5192-5198 (1990).

6 Kitzler, J., Hill, E., Hardman, R., et al. Analysis and quantitation of splicing variants of the TPA-inducible PGHS-1 mRNA in rat tracheal epithelial cells. Arch Biochem Biophys 316 856-863 (1995).

Funk, C.D., Funk, L.B., Kennedy, M.E., et al. Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment. FASEB J 5 2304-2312 (1991).

Smith, W.L., and Marnett, L.J. Prostaglandin endoperoxide synthase: Structure and catalysis. Biochim Biophys Acta 1083 1-17 (1991).

DeWitt, D.L., El-Harith, E.A., Kraemer, S.A., et al. The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases. J Biol Chem 265 5192-5198 (1990).

Marnett, L.J., and Maddipati, K.R. Prostaglandin H synthase. 293-334 (1991).

DeWitt, D.L., and Smith, W.L. Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence. Proc Natl Acad Sci USA 85 1412-1416 (1988).

Otto, J.C., and Smith, W.L. The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum. J Biol Chem 269 19868-19875 (1994).

Macchia, L., Di Paola, R., Guerrese, M., et al. Expression of prostaglandin endoperoxide H synthase 1 and 2 in human placenta at term. Biochem Biophys Res Commun 233 496-501 (1997).

Kitzler, J., Hill, E., Hardman, R., et al. Analysis and quantitation of splicing variants of the TPA-inducible PGHS-1 mRNA in rat tracheal epithelial cells. Arch Biochem Biophys 316 856-863 (1995).

Brock, T.G., McNish, R.W., and Peters-Golden, M. Arachidonic acid is preferentially metabolized by cyclooxygenase-2 to prostacyclin and prostaglandin E₂. J Biol Chem 274 11660-11666 (1999).

Cao, Y., Reddy, C.C., and Sordillo, L.M. Altered eicosanoid biosynthesis in selenium-deficient endothelial cells. Free Radic Biol Med 28 381-389 (2000).

Blanco, F.J., Guitian, R., Moreno, J., et al. Effect of antiinflammatory drugs on COX-1 and COX-2 activity in human articular chrondrocytes. J Rheumatol 26 1366-1373 (1999).

Rajnakova, A., Moochhala, S., Goh, P.M.Y., et al. Expression of nitric oxide synthase, cyclooxygenase, and p53 in different stages of human gastric cancer. Cancer Lett 172 177-185 (2001).

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