For immunochemical detection of COX-2
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COX-2 Rabbit Monoclonal Antibody (Clone RM348)

Item No. 42827

Product Insert (PDF)
Technical Information
Synonyms
  • Cyclooxygenase 2
  • PGHS-2
  • Prostaglandin H Synthase 2
Immunogen
A peptide corresponding to the C-terminus of human COX-2
Clone Designation
RM348
100 µl of protein A affinity-purified monoclonal antibody
Storage Buffer
PBS, with 50% glycerol, 1% BSA, and 0.09% sodium azide
Host
Rabbit
Isotype
IgG
Applications
IHC, WB
Cross Reactivity
(+) COX-2
Species Reactivity
(+) Human
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 (Item Nos. 90010 | 90010.1 | 10006607) 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 non-steroidal anti-inflammatory drug (NSAID) development. Cayman’s COX-2 Rabbit Monoclonal Antibody (Clone RM348) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.

    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).