Source: recombinant enzyme expressed in E. coli · M_r: 46 kDa · Specific activity: 2.2 units/mg · Protein concentration: 0.5 mg/ml · One unit of enzyme produces one µmole of prostaglandin D₂ (PGD₂)/min at 25°C in 100 mM Tris-HCl buffer, pH 8.0, containing 1 mM GSH, 1 mg/ml γ-globulin, and 40 µM PGH₂ · 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 and the hematopoietic enzyme.^1,2,3 L-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.¹ Cayman’s human recombinant L-PGDS is an active, highly-purified GST-fusion protein isolated from an E. coli expression system. Cysteines 89, 138, and 186 have been changed to alanines to prevent protein misfolding without affecting enzyme activity. The enzyme is ideally suited for a variety of biochemical experiments including mechanistic studies and development of selective enzyme inhibitors.

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

2 Urade, Y., and Hayaishi, O. Prostaglandin D synthase: Structure and function. Vitam Horm 58 89-120 (2000).

3 Urade, Y., and Eguchi, N. Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins Other Lipid Mediat 68-69 375-382 (2002).

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

Urade, Y., and Hayaishi, O. Prostaglandin D synthase: Structure and function. Vitam Horm 58 89-120 (2000).

Urade, Y., Tanaka, T., Eguchi, N., et al. Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase. J Biol Chem 270 1422-1428 (1995).

Irikura, D., Kumasaka, T., Yamamoto, M., et al. Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme. J Biochem 133 29-32 (2003).

Urade, Y., and Eguchi, N. Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins Other Lipid Mediat 68-69 375-382 (2002).

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