Antigen: mouse COX-2 amino acids 570-598 (DPQPTKTATINASASHSRLDDINPTVLIK) · Host: rabbit · Application(s): WB, IHC, and ICC · COX catalyzes the first step in the biosynthesis of prostaglandins, thromboxanes, and prostacyclins: the conversion of arachidonic acid to prostaglandin H₂. Recent discoveries of the induction of COX by a variety of stimuli such as phorbol esters, lipopolysaccharides, and cytokines led to the hypothosis that the inducible form of COX, COX-2, is responsible for the biosynthesis of prostaglandins under acute inflammatory conditions.^1,2 COX-2 is a 72 kDa protein which has been cloned from a variety of species including human, mouse, rat, and sheep.^3,4,5,6

1 Xie, W., Chipman, J.G., Robertson, D.L., et al. Expression of a mitogen-responsive gene encoding prostaglandin synthase is regulated by mRNA splicing. Proc Natl Acad Sci USA 88 2692-2696 (1991).

2 Smith, W.L., Garavito, R.M., and DeWitt, D.L. Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2. J Biol Chem 271 33157-33160 (1996).

3 Hla, T., and Neilson, K. Human cyclooxygenase-2 cDNA. Proc Natl Acad Sci USA 89 7384-7388 (1992).

4 Kujubu, D.A., Fletcher, B.S., Varnum, B.C., et al. TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue. J Biol Chem 266 12866-12872 (1991).

5 Olías, J.M., Rios, J.J., Valle, M., et al. Fatty acid hydroperoxide lyase in germinating soybean seedlings. J Agric Food Chem 38 624-630 (1990).

6 Zhang, V., O'Sullivan, M., Hussain, H., et al. Molecular cloning, functional expression, and selective regulation of ovine prostaglandin H synthase-2. Biochem Biophys Res Commun 227 499-506 (1996).

Morham, S.G., Langenbach, R., Loftin, C.D., et al. Prostaglandin synthase 2 gene disruption causes severe renal pathology in the mouse. Cell 83 473-482 (1995).

Langenbach, R., Morham, S.G., Tiano, H.F., et al. Prostaglandin synthase 1 gene disruption in mice reduces arachidonic acid-induced inflammation and indomethacin-induced gastric ulceration. Cell 83 483-492 (1995).

Harris, R.C., McKanna, J.A., Akai, Y., et al. Cyclooxygenase-2 is associated with the macula densa of rat kidney and increases with salt restriction. J Clin Invest 94 2504-2510 (1994).

Pomerantz, K.B., Summers, B., and Hajjar, D.P. Eicosanoid metabolism in cholesterol-enriched arterial smooth muscle cells. Evidence for reduced posttranscriptional processing of cyclooxygenase I and reduced cyclooxygenase II gene expression. Biochemistry 32 13624-13635 (1993).

Fletcher, B.S., Kujubu, D.A., Perrin, D.M., et al. Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional prostaglandin G/H synthase. J Biol Chem 267 4338-4344 (1992).

Yamagata, K., Andreasson, K.I., Kaufmann, W.E., et al. Expression of a mitogen-inducible cyclooxygenase in brain neurons: Regulation by synaptic activity and glucocorticoids. Neuron 11 371-386 (1993).

Smith, W.L., Garavito, R.M., and DeWitt, D.L. Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2. J Biol Chem 271 33157-33160 (1996).

Zhang, V., O'Sullivan, M., Hussain, H., et al. Molecular cloning, functional expression, and selective regulation of ovine prostaglandin H synthase-2. Biochem Biophys Res Commun 227 499-506 (1996).

Hla, T., and Neilson, K. Human cyclooxygenase-2 cDNA. Proc Natl Acad Sci USA 89 7384-7388 (1992).

Xie, W., Chipman, J.G., Robertson, D.L., et al. Expression of a mitogen-responsive gene encoding prostaglandin synthase is regulated by mRNA splicing. Proc Natl Acad Sci USA 88 2692-2696 (1991).

Kujubu, D.A., Fletcher, B.S., Varnum, B.C., et al. TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue. J Biol Chem 266 12866-12872 (1991).

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