For immunochemical detection of COX-1
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COX-1 (mouse) Polyclonal Antibody

Item No. 160109

Technical Information
Synonyms
  • Cyclooxygenase 1
  • PGHS-1
  • Prostaglandin Endoperoxide Synthase 1
  • Prostaglandin G/H Synthase 1
  • Prostaglandin H2 Synthase 1
500 µl of peptide affinity-purified polyclonal antibody
Storage Buffer
PBS, pH 7.2, with 50% glyercol and 0.02% sodium azide
Host
Rabbit
Applications
WB
Cross Reactivity
(-) COX-2 (all species)
Species Reactivity
(+) Human(+) Mouse(+) Ovine
UniProt Accession №
P22437
Origin
Animal/Rabbit
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Cyclooxygenase 1 (COX-1) is a bifunctional enzyme that exhibits both COX and peroxidase activities.1,2 It is composed of an N-terminal signal peptide, an EGF-like domain, a membrane binding domain, a catalytic domain, and a C-terminal tail.3 COX-1 is constitutively expressed in the gastrointestinal tract, kidney, spleen, liver, and lung and localizes to the endoplasmic reticulum.4,5 The COX component converts arachidonic acid (Item Nos. 90010 | 90010.1 | 10006607) to a hydroperoxyl endoperoxide prostaglandin G2 (PGG2; Item No. 17010) and the peroxidase component reduces the endoperoxide to the corresponding alcohol PGH2 (Item No. 17020), the precursor of PGs, thromboxanes, and prostacyclins.1,2 COX-1 is the target of many non-steroidal anti-inflammatory drugs (NSAIDs) and is responsible for the undesirable gastrointestinal and renal side effects, such as ulcer formation and reductions in the glomerular filtration rate, respectively.6,7 Cayman’s COX-1 (mouse) Polyclonal Antibody can be used for Western blot (WB).

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Nugteren, D.H., and Hazelhof, E. Isolation and properties of intermediates in prostaglandin biosynthesis. Biochim. Biophys. Acta 326(3), 448-461 (1973).

    2. Hamberg, M., and Samuelsson, B. Detection and isolation of an endoperoxide intermediate in prostaglandin biosynthesis. Proc. Natl. Acad. Sci. USA 70(3), 899-903 (1973).

    3. Smith, W.L., and DeWitt, D.L. Prostaglandin endoperoxide H synthases-1 and -2. Adv. Immunol. 62, 167-215 (1995).

    4. Seibert, K., Zhang, Y., Leahy, K., et al. Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain. Proc. Natl. Acad. Sci. USA 91(25), 12013-12017 (1994).

    5. Morita, I., Schindler, M., Regier, M.K., et al. Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2. The Journal of Biological Chemisty 270(18), 10902-10908 (1995).

    6. Gierse, J.K., Hauser, S.D., Creely, D.P., et al. Expression and selective inhibition of the constitutive and inducible forms of human cyclo-oxygenase. Biochem. J. 305(Pt. 2), 379-484 (1995).

    7. Frölich, J.C. A classification of NSAIDs according to the relative inhibition of cyclooxygenase isoenzymes. Trends Pharmacol. Sci. 18(1), 30-34 (1997).

    Product Citations

    Matsumoto, T., Kobayashi, S., Ando, M., et al. Alteration of vascular responsiveness to uridine adenosine tetraphosphate in aortas Isolated from male diabetic otsuka long-evans tokushima fatty rats: The involvement of prostanoids. Int. J. Mol. Sci. 18(11), E2378 (2017).

    Björk, W., Mirrasekhian, E., Zajdel, J., et al. Cyclooxygenase isoform exchange blocks brain-mediated inflammatory symptoms. PLoS One 11(11), e0166153 (2016).

    Apostoli, A.J., Skelhorne-Gross, G.E., Rubino, R.E., et al. Loss of PPARcexpression in mammary secretory epithelial cellscreates a pro-breast tumorigenic environment. Int. J. Cancer 134(5), 1055-1066 (2014).

    de Faria, F.M., Luiz-Ferreira, A., Socca, E.A., et al. Effects of rhizophora mangle on experimental colitis induced by TNBS in rats. Evid Based Complement. Med. 2012, 753971 (2012).

    Chia, E., Kagota, S., Wijekoon, E.P., et al. Protection of protease-activated receptor 2 mediated vasodilatation against angiotensin II-induced vascular dysfunction in mice. BMC Pharmacol. 11, 10 (2011).

    Wu, T., Wu, H., Wang, J., et al. Expression and cellular localization of cyclooxygenases and prostaglandin E synthases in the hemorrhagic brain. J. Neuroinflammation 8, 22 (2011).

    Seta, F., Rahmani, M., Turner, P.V., et al. Pulmonary oxidative stress is increased in cyclooxygenase-2- knockdown mice with mild pulmonary hypertension induced by monocrotaline. PLoS One 6(8), e23439 (2011).

    Lazarus, M., Munday, C.J., Eguchi, N., et al. Immunohistochemical localization of microsomal PGE synthase-1 and cyclooxygenases in male mouse reproductive organs. Endocrinology 143(6), 2410-2419 (2002).

    Kim, D.W., Chi, Y.S., Son, K.H., et al. Effects of sophoraflavanone G, a prenylated flavonoid from Sophora flavescens, on cyclooxygenase-2 and in vivo inflammatory response. Arch. Pharm. Res. 25(3), 329-335 (2002).