For immunochemical detection of COX-2
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COX-2 (human) Polyclonal Antibody

Item No. 160107

Technical Information
Synonyms
  • Cyclooxygenase 2
  • PGHS-2
  • Prostaglandin H Synthase 2
Immunogen
Peptide from the C-terminal region of human COX-2
MW
72 kDa
500 μg protein A-purified polyclonal antibody
Storage Buffer
PBS, pH 7.2, with 50% glycerol and 0.02% sodium azide
Host
Rabbit
Applications
IF, WB
Cross Reactivity
(+) COX-2(-) COX-1
Species Reactivity
(+) Human(+) Mouse(+) Ovine
UniProt Accession №
P35354
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 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). COX2 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.3,4 Thus, COX-2 has been the focus of attention for nonsteroidal anti-inflammatory drug (NSAID) development. Cayman's COX-2 (human) Polyclonal Antibody can be used for immunofluorescence (IF) and Western blot (WB) applications. The antibody recognizes a unique C-terminal region of COX-2 that is not present in COX-1, specifically detecting COX-2 at 72 kDa from human, mouse, and ovine samples.

    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. Kang, Y.-J., Mbonye, U.R., DeLong, C.J., et alRegulation of intracellular cyclooxygenase levels by gene transcription and protein degradation. Prog. Lipid Res. 46(2), 108-125 (2007).

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

    Product Citations

    Yamazaki, R., Kawai, S., Matsumoto, T., et alHydrolytic activity is essential for aceclofenac to inhibit cyclooxygenase in rheumatoid synovial cells. J. Pharmacol. Exp. Ther. 289(2), 676-681 (1999).

    Zhuang, Y., Wang, C., Wu, C., et alMitochondrial oxidative stress activates COX-2/mPGES-1/PGE2 cascade induced by albumin in renal proximal tubular cells. Oncotarget 9(10), 9235-9245 (2018).

    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).

    Agra Andrieu, N., Motiño, O., Mayoral, R., et alCyclooxygenase-2 is a target of microRNA-16 in human hepatoma cells. PLoS One 7(11), e50935 (2012).

    Lalier, L., Pedelaborde, F., Braud, C., et alIncrease in intracellular PGE2 induces apoptosis in Bax-expressing colon cancer cell. BMC Cancer 11, 153 (2011).

    Sobrino, A., Mata, M., Laguna-Fernandez, A., et alEstradiol stimulates vasodilatory and metabolic pathways in cultured human endothelial cells. PLoS One 4(12), e8242 (2009).

    Gauthier, M.L., Berman, H.K., Miller, C., et alAbrogated response to cellular stress identifies DCIS associated with subsequent tumor events and defines basal-like breast tumors. Cancer Cell. 12(5), 479-491 (2007).

    Nantel, F., Meadows, E., Denis, D., et alImmunolocalization of cyclooxygenase-2 in the macula densa of human elderly. FEBS Lett. 457(3), 475-477 (1999).