Source: human recombinant N-terminal histadine-tagged protein; purified from an E. coli overexpression system · M_r: 24.3 kDa · Specific activity: XX units/mg · Protein concentration: XX mg/ml · One unit of enzyme produces one µmole of PGD₂/min at 25°C in 100 mM Tris-HCl buffer, pH 8.0, containing 1 mM GSH, 1 mg/ml magnesium chloride, and 40 µM PGH₂ · 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.^1,2,3,4 Hematopoietic PGD synthase (H-PGDS) is widely distributed in the peripheral tissues and is localized in the antigen-presenting cells, mast cells, and megakaryocytes. PGD₂ is produced by H-PGDS in large quantities by allergen-stimulated mast cells and acts as a pro-inflammatory mediator in allergic reactions. H-PGDS requires glutathione for activity and belongs to the sigma-class of glutathione-S-transferases.^1,4,5 Cayman Chemical’s H-PGDS is a highly-purified, active recombinant enzyme isolated from an E. Coli expression system. The enzyme is ideally suited for a variety of biochemical experiments including mechanistic studies and development of selective enzyme inhibitors.

1 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).

2 Jowsey, I.R., Thomson, A.M., Flanagan, J.U., et al. Mammalian class sigma glutathione s-transferases: Catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D₂ synthases. Biochem J 359 507-516 (2001).

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

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

5 Urade, Y., Fujimoto, N., Ujihara, M., et al. Biochemical and immunological characterization of rat spleen prostaglandin D synthetase. J Biol Chem 262(8) 3820-3825 (1987).

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).

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

Urade, Y., Fujimoto, N., Ujihara, M., et al. Biochemical and immunological characterization of rat spleen prostaglandin D synthetase. J Biol Chem 262(8) 3820-3825 (1987).

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

Jowsey, I.R., Thomson, A.M., Flanagan, J.U., et al. Mammalian class sigma glutathione s-transferases: Catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D₂ synthases. Biochem J 359 507-516 (2001).

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