Antigen: bovine PGIS amino acids 299-329 (LLKNPEALAAVRGELETVLLGAEQPISQMTT) · Host: rabbit · Application(s): WB and IP; other applications not tested · Prostaglandin I synthase (PGIS) catalyzes the isomerization of PGH₂ to PGI₂. PGI₂ (prostacyclin) is a potent vasodilator and inhibitor of platelet aggregation. PGIS is a membrane-bound hemoprotein localized primarily in endothelial cells.¹ The cloned bovine and human enzymes contain 500 amino acids and a calculated molecular mass of 56,629 and 57,103, respectively.^2,3,4 Northern blot analysis reveals that the mRNA for PGIS is expressed in a wide variety of human tissues and is particularly abundant in ovary, heart, skeletal muscle, lung, and prostate.²

1 DeWitt, D.L., and Smith, W.L. Purification of prostacyclin synthase from bovine aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein. J Biol Chem 258 3285-3293 (1983).

2 Miyata, A., Hara, S., Yokoyama, C., et al. Molecular cloning and expression of human prostacyclin synthase. Biochem Biophys Res Commun 200 1728-1734 (1994).

3 Pereira, B., Wu, K.K., and Wang, L. Molecular cloning and characterization of bovine prostacyclin synthase. Biochem Biophys Res Commun 203 59-66 (1994).

4 Hara, S., Miyata, A., Yokoyama, C., et al. Isolation and molecular cloning of prostacyclin synthase from bovine endothelial cells. J Biol Chem 269 19897-19903 (1994).

DeWitt, D.L., and Smith, W.L. Purification of prostacyclin synthase from bovine aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein. J Biol Chem 258 3285-3293 (1983).

Pereira, B., Wu, K.K., and Wang, L. Molecular cloning and characterization of bovine prostacyclin synthase. Biochem Biophys Res Commun 203 59-66 (1994).

Hara, S., Miyata, A., Yokoyama, C., et al. Isolation and molecular cloning of prostacyclin synthase from bovine endothelial cells. J Biol Chem 269 19897-19903 (1994).

Miyata, A., Hara, S., Yokoyama, C., et al. Molecular cloning and expression of human prostacyclin synthase. Biochem Biophys Res Commun 200 1728-1734 (1994).

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