Active, pure human recombinant enzyme
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COX-2 (human, recombinant)

Item No. 60122

Technical Information
Synonyms
  • Cyclooxygenase 2
  • Prostaglandin H Synthase 2
Purity
≥75% (estimated by SDS-PAGE)
Source
Active recombinant N-terminal His-tagged COX-2N580A mutant purified from insect cells
Amino Acids
20-604
MW
67.9 kDa
80 mM Tris, pH 8.0, with 0.3 mM DDC, 0.01% Tween 20, and 10% glycerol
Specific Activity
>8,000 U/mg
UniProt Accession №
P35354
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Cyclooxygenase 2 (COX-2) is a bifunctional enzyme that exhibits both COX and peroxidase activities and catalyzes the first step in the biosynthesis of prostaglandins, thromboxanes, and prostacyclins.1,2 The COX component converts arachidonic acid to the hydroperoxy endoperoxide prostaglandin G2 (PGG2; Item No. 17010), and the peroxidase component reduces the endoperoxide to the corresponding alcohol PGH2 (Item No. 17020). COX-2 expression is induced by a variety of stimuli, including phorbol esters, LPS, and cytokines and is responsible for the biosynthesis of PGs under acute inflammatory conditions.3 Thus, COX-2 has been the focus of attention for the nonsteroidal anti-inflammatory drug (NSAID) development. Cayman's COX-2 (human, recombinant) contains an N-terminal hexahistidine tag and an alanine substituted for asparagine at position 580 (COX-2N580A) that prevents glycosylation at position 580 and decreases enzyme degradation in cells.4

    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. Blobaum, A.L., and Marnett, L.J. Structural and functional basis of cyclooxygenase inhibition. J. Med. Chem. 50(7), 1425-1441 (2007).

    4. Sevigny, M.B., Li, C.-F., Alas, M., et alGlycosylation regulates turnover of cyclooxygenase-2. FEBS Lett. 580(28-29), 6533-6536 (2006).

    Product Citations

    Zhao-Yong, Y., Zhi-Fei, Z., Xiao-Bo, H., et alStudy on the effect of amicoumacin B on up-regulating bmp-2 transcription and expression in MG63 cells. Chin. J. Antibiot. 33(4), 203-205 (2008).

    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).

    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).