Technical Data
P9053-25P
Prostaglandin D Synthase, Hematopoietic form (PGD Synthase)
Description:
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 ( -trace) and the hematopoietic enzyme. 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. Hematopoietic PGD synthase 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 approximately 23kD in size.

Applications:
Suitable for use in Immunohistochemistry and Western Blot. Other applications not tested.

Recommended Dilutions:
Immunohistochemistry: 1:1000-1:5000
Western Blot: 1:1000. Incubate for 1 hour at RT or overnight at 4C for optimal results..
Optimal dilution determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
MabIgG6D697Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceMouseRat
Concentration:
~1mg/ml
Immunogen:
Recombinant protein corresponding to mouse hematopoietic prostaglandin D synthase (H-PGDS).
Purity:
Purified
Form
Supplied as a liquid in PBS, pH 7.2, 0.1% BSA, 0.02% sodium azide, 50% glycerol.
Specificity:
Recognizes mouse H-PGDS. Species Crossreactivity: human.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1.Urade, Y., Watanabe, K., and 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).