10006788  Prostaglandin D Synthase (lipocalin-type; human recombinant)

L-PGDS; Lipocalin-PGDS


Chemical structure definitions are available for many Cayman products. See Chemical Structure Database for details.

Source: recombinant enzyme expressed in E. coli · Mr: 46 kDa · 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., Hayaishi, O. Prostaglandin D, E, and F synthases. J Lipid Mediat Cell Signal 12 257-273 (1995).
2  Urade, Y., Hayaishi, O. Prostaglandin D synthase: Structure and function. Vitamins and Hormones 58 89-120 (2000).
3  Urade, Y., Eguchi, N. Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins and Other Lipid Mediators 68-69, 375-382 (2002).


Purchase 10006788 Prostaglandin D Synthase (lipocalin-type; human recombinant)

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Warning This product is not for human or veterinary use.

Pricing updated 2010-03-14.
Prices are subject to change without notice.

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