Nitrotyrosine Monoclonal Antibody (Clone CC.22.8C7.3)

Nitrotyrosine is a post-translational modification that is formed by the nitration of tyrosine.¹ Under conditions of oxidative stress, tyrosine is oxidized by reactive oxygen species (ROS) or, in the presence of hydrogen peroxide and nitrite, by myeloperoxidase (MPO) to yield a tyrosine radical that reacts with reactive nitrogen species (RNS), such as nitric oxide or peroxynitrite, to form nitrotyrosine. It exists in a free or protein-bound form and is commonly used as a marker of nitrosative or oxidative stress.² Nitrotyrosine residues have been found in a variety of proteins, including LDL, surfactant protein A, angiotensin II, and human and bovine serum albumin.³ Free nitrotyrosine production induced by peroxynitrite is inhibited by the polyphenols epicatechin gallate, gallic acid, catechin, or epicatechin in cell-free assays, as well as in aortic rings isolated from normotensive and spontaneously hypertensive rats administered the antioxidant N-acetyl-cysteine (NAC; Item No. 20261).^4,5 Nitrotyrosine levels are increased in the affected tissues of numerous pathological conditions, including atherosclerosis, cancer, ulcerative colitis, Alzheimer's disease, and Parkinson's disease.³ Autoantibodies that recognize nitrotyrosinated proteins are increased in the synovium of patients with rheumatoid arthritis and are positively correlated with joint and tendon inflammation.¹ Cayman's Nitrotyrosine Monoclonal Antibody (Clone CC.22.8C7.3) can be used for ELISA and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Smallwood, M.J., Nissim, A., Knight, A.R., et al. Oxidative stress in autoimmune rheumatic diseases. Free Radic. Biol. Med. 125, 3-14 (2018).

2. Teixeira, D., Fernandes, R., Prudêncio, C., et al. 3-Nitrotyrosine quantification methods: Current concepts and future challenges. Biochimie 125, 1-11 (2016).

3. Oldreive, C., and Rice-Evans, C. The mechanisms for nitration and nitrotyrosine formation in vitro and in vivo: Impact of diet. Free Radic. Res. 35(3), 215-231 (2001).

4. Pannala, A.S., Rice-Evans, C.A., Halliwell, B., et al. Inhibition of peroxynitrite-mediated tyrosine nitration by catechin polyphenols. Biochem. Biophys. Res. Commun. 232(1), 164-168 (1997).

5. Cabassi, A., Dumont, E.C., Girouard, H., et al. Effects of chronic N-acetylcysteine treatment on the actions of peroxynitrite on aortic vascular reactivity in hypertensive rats. J. Hypertens. 19(7), 1233-1244 (2001).

Ahn, B.H., Coblentz, P.D., Beharry, A.W., et al. Diaphragm abnormalities in patients with end-stage heart failure: NADPH oxidase upregulation and protein oxidation. Front. Physiol. 686, (2017).

Magder, S., Parthenis, D.G., and Ghouleh, I.A. Preservation of renal blood flow by the antioxidant EUK-134 in LPS-treated pigs. Int. J. Mol. Sci. 16(4), 6801-6817 (2015).

Negrette-Guzmán, M., Huerta-Yepez, S., Medina-Campos, O.N., et al. Sulforaphane attenuates gentamicin-induced nephrotoxicity: Role of mitochondrial protection. Evid. Based Complement. Alternat. Med. 135314, (2013).

Fajardo, V.A., Bombardier, E., McMillan, E., et al. Phospholamban overexpression in mice causes a centronuclear myopathy-like phenotype. Dis. Model Mech. 8(8), 999-1009 (2015).

Szalay, C.I., Erdélyi, K., Kökény, G., et al. Oxidative/nitrative stress and inflammation drive progression of doxorubicin-induced renal fibrosis in rats as revealed by comparing a normal and a fibrosis-resistant rat strain. PLoS One 10(6), e0127090 (2015).