References |
Synonyms |
|
Formulation |
200 µl polyclonal antiserum containing 0.02% sodium azide |
Stability |
6 months |
Storage |
-20°C |
Shipping |
Wet ice
in continental US; may vary elsewhere
|
Specificity |
Human H-PGD synthase |
+ |
Mouse H-PGD synthase |
+ |
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Background Reading
Urade, Y., Watanabe, K., and Hayaishi, O. Prostaglandin D, E, and F synthases. J Lipid Mediat Cell Signal 12 257-273 (1995).
Toh, H., Kubodera, H., Nakajima, N., et al. Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins. Protein Eng 9 1067-1082 (1996).
Zahn, M., Mäder, A., Schmidt, B., et al. Purification and N-terminal sequence of β-trace, a protein abundant in human cerebrospinal fluid. Neurosci Lett 154 93-95 (1993).
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).
Kanaoka, Y., Ago, H., Inagaki, E., et al. Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell 90 1085-1095 (1997).
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Size |
Global Purchasing |
1 ea |
|
Description
Antigen:
recombinant mouse H-PGD synthase
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Host:
rabbit
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Application(s):
WB and IHC
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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 (β-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 β-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 kDa in size.5,3 Cayman Chemical’s H-PGD synthase polyclonal antibody can be used for western blot and immunohistochemical analysis for H-PGD synthase on samples of human and mouse origin. Other applications for use of this antibody have not yet been tested.
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 Eng 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., Mäder, A., Schmidt, B., et al. Purification and N-terminal sequence of β-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).
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