Antigen: recombinant mouse H-PGD synthase · Clone designation: 7H4 · Host: rat · Application(s): WB and IHC · 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.^1,2,3 Lipocalin-type PGD synthase 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.^4,2 Hematopoietic PGD synthase 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.^5,3 Cayman Chemical’s H-PGD synthase polyclonal antibody can be used for western blot and immunohistochemical analysis for H-PGD synthase on samples of human and mouse origin. Other applications for use of this antibody have not yet been tested.

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).

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

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).

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).

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

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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