Active • Source: Ram seminal vesicles • AA: full length • MW: 70 kDa
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

COX-1 (ovine)

Item No. 60100

Technical Information
Synonyms
  • Cyclooxygenase 1
  • PGHS-1
  • Prostaglandin Endoperoxide Synthase 1
  • Prostaglandin G/H Synthase 1
  • Prostaglandin H2 Synthase 1
Source
Active COX-1 isolated from ram seminal vesicles
Amino Acids
Full length
MW
70 kDa
80 mM Tris-HCl, pH 8.0, containing 0.3 mM DDC, 0.1% polysorbate 20, and 10% glycerol
UniProt Accession №
P05979
Origin
Animal/Ram
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    Add

    Lipid Resource Center
    Discover Products & Resources for Lipid Research
    • High-purity lipid standards
    • Lipid roles in biology
    • Lipids in health & disease
    • Lipids for pharmaceutical development
    • Protocols, advice, & resources
    EXPLORE NOW
    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 (ovine) protein can be used for enzyme activity assays.

    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 alPharmacological 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 alDifferent 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 alExpression 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

    Van Anh, T.T., Mostafa, A., Rao, Z., et alFrom Vietnamese plants to a biflavonoid that relieves inflammation by triggering the lipid mediator class switch to resolution. Acta Pharm. Sin. B. 11(6), 1629-1647 (2021).

    Beeghly-Fadiel, A., Wilson, A.J., Keene, S., et alDifferential cyclooxygenase expression levels and survival associations in type I and type II ovarian tumors. J. Ovarian Res. 11(17), (2018).

    Hinz, C., Aldrovandi, M., Uhlson, C., et alHuman platelets utilize cycloxygenase-1 to generate dioxolane A3, a neutrophil-activating eicosanoid. The Journal of Biological Chemisty 291(26), 13448-13464 (2016).

    Gouveia-Figueira, S., Karlsson, J., Deplano, A., et alCharacterisation of (R)-2-(2-fluorobiphenyl-4-yl)-N-(3-methylpyridin-2-yl)propanamide as a dual fatty acid amide hydrolase: Cyclooxygenase inhibitor. PLoS One 10(9), e0139212 (2015).

    Karlsson, J., and Fowler, C.J. Inhibition of endocannabinoid metabolism by the metabolites of ibuprofen and flurbiprofen. PLoS One 9(7), e103589 (2014).

    Hoobler, E.K., Warrilow, A.G., Perry, S.C., et alDiscovery of a novel dual fungal CYP51/human 5-lipoxygenase inhibitor: implications for anti-fungal therapy. PLoS One 8(6), e65928 (2013).

    Landa, P., Kutil, Z., Temml, V., et alRedox and non-redox mechanism of in vitro cyclooxygenase inhibition by natural quinones. Planta Med. 78(4), 326-333 (2011).

    Pestchanker, M.J., and Giordano, O.S. Pyrrolizidine alkaloids from five senecio species. J. Nat. Prod. 49(4), 722-723 (1986).

    Esser, R., Berry, C., Du, Z., et alPreclinical pharmacology of lumiracoxib: a novel selective inhibitor of cyclooxygenase-2. Br. J. Pharmacol. 144(4), 538-550 (2005).

    Selvam, C., Jachak, S.M., and Bhutani, K.K. Cyclooxygenase inhibitory flavonoids from the stem bark of Semecarpus anacardium Linn. Phytother. Res. 18(7), 582-584 (2004).

    Kim, Y.P., Yamada, M., Lim, S.S., et alInhibition by tectorigenin and tectoridin of prostaglandin E2 production and cyclooxygenase-2 induction in rat peritoneal macrophages. Biochim. Biophys. Acta 1438(3), 399-407 (1999).