Technical Data
Prostaglandin D Synthase, Hematopoietic form (PGD Synthase)
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 (beta-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 beta-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 kD in size.

Suitable for use in Immunohistochemistry and Western Blot. Other applications have not been tested.

Recommended Dilutions:
Immunohistochemistry: 1:1000
Western Blot: 1:200 with 1 hour incubation at RT. (1:500 dilution with overnight incubation at 4C also produces optimal results.)
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
1Vial4C (-20C Glycerol)Blue IceHumanRabbit
Recombinant human hematopoietic prostaglandin D synthase (H-PGDS).
Purified by Protein A affinity chromatography.
Supplied as a liquid in TBS, pH 7.4, 0.1% BSA, 0.02% sodium azide, 50% glycerol.
Recognizes human H-PGDS. Species Crossreactivity: mouse
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1 Urade, Y., Watanabe, K., 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 Engineering 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., Mder, A., Schmidt, B., et al. Purification and N-terminal sequence of -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).