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Application(s):
positive control for WB
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Source:
human recombinant protein expressed in E. coli
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Mr:
23.3 kDa
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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 (β-trace) and the hematopoietic enzyme.1,2,3,4 Lipocalin-type 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.3,4 Hematopoietic-PGDS is widely distributed in the peripheral tissues and is localized in the antigen-presenting cells, mast cells, and megakaryocytes. This enzyme, which requires glutathione for activity, belongs to the sigma-class of Glutathione-S-Transferases and is implicated in allergic and inflammatory diseases.1,5,4
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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., 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).
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