Antigen: human hematopoietic-type PGDS amino acids 30-41 (EDHRIEQADWPE) · Host: rabbit · Application(s): WB · Prostaglandin D synthase (PGDS) catalyzes the isomerization of PGH₂ to produce PGD₂. PGD₂ induces sleep, regulates nociception, inhibits platelet aggregation, and acts as an allergic mediator. Two distinct types of PGDS have been identified, namely the lipocalin type enzyme (β-trace) and the hematopoietic enzyme.^1,2,3 Lipocalin type PGDS is localized in the central nervous system and male genital organs of various mammals and the human heart. This enzyme has been identified as β-trace, which is a major protein in human cerebrospinal fluid.^2,4 Hematopoietic PGDS is widely distributed in the peripheral tissues and is localized in the antigen-presenting cells, mast cells, and megakaryocytes.¹ This enzyme, which requires glutathione for activity, belongs to the sigma-class of glutathione-S-transferases and is approximately 23 kDa in size.⁵

1 Urade, Y., Watanabe, K., and Hayaishi, O. Prostaglandin D, E, and F synthases. J Lipid Mediat Cell Signal 12 257-273 (1995).

2 Toh, H., Kubodera, H., Nakajima, N., et al. Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins. Protein Eng 9 1067-1082 (1996).

3 Kanaoka, Y., Ago, H., Inagaki, E., et al. Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell 90 1085-1095 (1997).

4 Zahn, M., Mäder, A., Schmidt, B., et al. Purification and N-terminal sequence of β-trace, a protein abundant in human cerebrospinal fluid. Neurosci Lett 154 93-95 (1993).

5 Kanaoka, Y., Fujimori, K., Kikuno, R., et al. Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Eur J Biochem 267 3315-3322 (2000).

Zahn, M., Mäder, A., Schmidt, B., et al. Purification and N-terminal sequence of β-trace, a protein abundant in human cerebrospinal fluid. Neurosci Lett 154 93-95 (1993).

Toh, H., Kubodera, H., Nakajima, N., et al. Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins. Protein Eng 9 1067-1082 (1996).

Melegos, D.N., Diamandis, E.P., Oda, H., et al. Immunofluorometric assay of prostaglandin D synthase in human tissue extracts and fluids. Clin Chem 42 1984-1991 (1996).

Tokugawa, Y., Kunishige, I., Kuboto, Y., et al. Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma. Biol Reprod 58 600-607 (1998).

Urade, Y., Watanabe, K., and Hayaishi, O. Prostaglandin D, E, and F synthases. J Lipid Mediat Cell Signal 12 257-273 (1995).

Kanaoka, Y., Fujimori, K., Kikuno, R., et al. Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Eur J Biochem 267 3315-3322 (2000).

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