Antigen:
purified ovine COX-1
·
Host:
rabbit
·
Application(s):
WB and IHC
·
Cyclooxygenase catalyzes the first step in the biosynthesis of prostaglandins, thromboxanes, and prostacyclins: the conversion of arachidonic acid to prostaglandin H2 COX-1 is constitutively expressed in almost all animal tissues and is involved in the homeostatic role of eicosanoids.1,2 Recent discoveries of the induction of cyclooxygenase biosynthesis by a variety of stimuli such as phorbol esters, lipopolysaccharides, and cytokines led to the hypothesis that the inducible form of cyclooxygenase, COX-2, is responsible for the biosynthesis of prostaglandins under acute inflammatory conditions.3 COX-1 and -2 are 70 and 72 kDa proteins, respectively. Both cyclooxygenases have been cloned from a variety of species including human, mouse, rat, and sheep.4,5 COX-1 isoform at the amino acid level, whereas the homology between COX-1 and COX-2 is only about 60%.
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
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).
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
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).
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).
Zheng, D., Fu, S.J., Lysz, T.W., et al. Immunocytochemical localization of cyclooxygenase in the rat lens. Invest Ophthamol Vis Sci 33 178-183 (1992).
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).
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).
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).
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).
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