For immunochemical detection of PGIS
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Prostaglandin I Synthase Monoclonal Antibody (Clone 3C8)

Item No. 10247

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • PGIS
  • Prostacyclin Synthase
Immunogen
Cell surface PGIS from follicular dendritic cell line HK
Clone Designation
3C8
Formulation (Request formulation change)
200 µg of lyophilized protein G-purified monoclonal antibody
Storage Buffer
TBS, pH 7.4 when resuspended in 500 µl double distilled water
Host
Mouse
Isotype
IgG1
Applications
FC, ICC, IHC, IP, WB
Species Reactivity
(+) Human(+) Mouse(+) Rat
License
Sold under license from Kangwon National University
UniProt Accession №
Q16647
Origin
Animal/Mouse
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    1 ea (200 µg)

    $347

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    Product Description

    Prostaglandin I synthase (PGIS) catalyzes the isomerization of PGH2 to PGI2. PGI2 (prostacyclin) is a potent vasodilator and inhibitor of platelet aggregation. PGIS is a membrane-bound hemoprotein localized primarily in endothelial cells.1 The cloned bovine and human enzymes contain 500 amino acids and a calculated molecular mass of 56,629 and 57,103, respectively.2,3,4 Northern blot analysis reveals that the mRNA for PGIS is expressed in a wide variety of human tissues and is particularly abundant in ovary, heart, skeletal muscle, lung, and prostate.2

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Miyata, A., Hara, S., Yokoyama, C., et al. Molecular cloning and expression of human prostacyclin synthase. Biochem. Biophys. Res. Commun. 200(3), 1728-1734 (1994).

    2. Pereira, B., Wu, K.K., and Wang, L.H. Molecular cloning and characterization of bovine prostacyclin synthase. Biochem. Biophys. Res. Commun. 203(1), 59-66 (1994).

    3. Hara, S., Miyata, A., Yokoyama, C., et al. Isolation and molecular cloning of prostacyclin synthase from bovine endothelial cells. The Journal of Biological Chemisty 269(31), 19897-19903 (1994).

    4. DeWitt, D.L., and Smith, W.L. Purification of prostacyclin synthase from bovine aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein. The Journal of Biological Chemisty 258(5), 3285-3293 (1983).