COX-1 Monoclonal Antibody (Clone CX111)

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 Monoclonal Antibody (Clone CX111) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

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).

Shojo, H., Borlongan, C.V., and Mabuchi, T. Genetic and histological alterations reveal key role of prostaglandin synthase and cyclooxygenase 1 and 2 in traumatic brain Injury-induced neuroinflammation in the cerebral cortex of rats exposed to moderate fluid percussion injury. Cell Transplant 26(7), 1301-1313 (2017).

Bhatt, D.P., Puig, K.L., Gorr, M.W., et al. A pilot study to assess effects of long-term inhalation of airborne particulate matter on early Alzheimer-like changes in the mouse brain. PLoS One 10(5), e0127102 (2015).

Wobst, I., Schiffmann, S., Birod, K., et al. Dimethylcelecoxib inhibits prostaglandin E₂ production. Biochem. Pharmacol. 76(1), 62-69 (2008).

Petzold, G.C., Albeanu, D.F., Sato, T.F., et al. Coupling of neural activity to blood flow in olfactory glomeruli is mediated by astrocytic pathways. Neuron. 58(6), 897-910 (2008).

Deeb, R.S., Shen, H., Gamss, C., et al. Inducible nitric oxide synthase mediates prostaglandin H₂ synthase nitration and suppresses eicosanoid production. Am. J. Pathol. (168(1), 349-362 (2006).