Antigen: human lipocalin-type PGD synthase amino acids 30-41 (VQPNFQPDKFLG) · Host: rabbit · Application(s): WB; other applications not tested · Prostaglandin D synthase (PGD synthase) 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 PGD synthase have been identified, namely the lipocalin-type enzyme (β-trace) and the hematopoietic enzyme.^1,2 Lipocalin-type PGD synthase is localized in the central nervous system and male genital organs of various mammals and the human heart whereas the hematopoietic PGD synthase is widely distributed in the peripheral tissues and localized in the antigen-presenting cells, mast cells, and megakaryocytes.^1,3,4,5 The lipocalin-type PGD synthase has been identified as β-trace, which is a major protein in human cerebrospinal fluid.^2,6 Human lipocalin-type PGD synthase is a 190 amino acid protein with a calculated molecular weight of 21,016.⁷

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 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).

4 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).

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).

6 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).

7 Nagata, A., Suzuki, Y., Igarashi, M., et al. Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins. Proc Natl Acad Sci USA 88 4020-4024 (1991).

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).

Nagata, A., Suzuki, Y., Igarashi, M., et al. Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins. Proc Natl Acad Sci USA 88 4020-4024 (1991).

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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