Nitrotyrosine Affinity Sorbent
Item № 389549
200 µg $259.00 $0.00

Pricing updated 2015-11-30. Prices are subject to change without notice.

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The Nitrotyrosine Affinity Sorbent is designed for IP of nitrated proteins from biological samples. This is an effective way to concentrate nitrated proteins for subsequent detection by a different anti-nitrotyrosine antibody, such as Cayman’s nitrotyrosine polyclonal antibody (Catalog No. 189540), by WB analysis. Nitric oxide (NO) is a product of the enzymatic conversion of arginine to citrulline by nitric oxide synthase. NO reacts rapidly with superoxide (6.7 x 109 M−1sec−1) to form peroxynitrite. At physiological pH and in the presence of transition metals, peroxynitrite undergoes heterolytic cleavage to form hydroxyl anion and nitronium ion, the latter of which nitrates protein tyrosine residues. Thus, the presence of nitrotyrosine on proteins can be used as a marker for peroxynitrite formation in vivo.1,2 Nitrotyrosine has been shown to be present in proteins from a variety of clinical conditions including artherosclerotic lesions of human coronary arteries, postischemic heart, and placenta during preeclampsia.3,4,5 Increased nitration of proteins in motor neurons has been identified in patients with ALS (amyotrophic lateral sclerosis) and may be due to mutations in superoxide dismutase.2,6,7,8

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Technical Information
Formulation 200 μg of anti-Nitrotyrosine Monoclonal Antibody (Item No. 189542) coupled to protein A agarose; supplied as a 50% slurry in TBS, pH 7.4 with 0.02% sodium azide

WARNING - This product is not for human or veterinary use.

Shipping & Storage
Storage 4°C
Shipping Wet ice in continental US; may vary elsewhere
Stability 1 year
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Download Product Insert 87 Kb PDF

Download Safety Data Sheet (SDS) 25 Kb PDF

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Additional Information

View the Cayman Structure Database for chemical structure definitions for many Cayman products

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References & Background Reading
Product Description References

1. Beckman, J.S., Chen, J., Ischiropoulos, H., et al. Oxidative chemistry of peroxynitrite. Methods Enzymol 233 229-240 (1994).

2. Beckman, J.S., and Koppenol, W.H. Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and the ugly. Am J Physiol 271 C1424-C1437 (1996).

3. Beckman, J.S., Ye, Y.Z., Anderson, P.G., et al. Extensive nitration of protein tyrosines in human atherosclerosis detected by immunohistochemistry. Biol Chem Hoppe-Seyler 375 81-88 (1994).

4. Wang, P., and Zweier, J.L. Measurement of nitric oxide and peroxynitrite generation in the postischemic heart. Evidence for peroxynitrite-mediated reperfusion injury. J Biol Chem 271 29223-29230 (1996).

5. Myatt, L., Rosenfield, R.B., Eis, A.L.W., et al. Nitrotyrosine residues in placenta. Evidence of peroxynitrite formation and action. Hypertension 28 488-493 (1996).

6. Abe, K., Pan, L., Watanabe, M., et al. Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis. Neurol Res 19 124-128 (1997).

7. Chou, S.M., Wang, H.S., and Komai, K. Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: An immunohistochemical study. J Chem Neuroanat 10 249-258 (1996).

8. Ferrante, R.J., Shinobu, L.A., Schulz, J.B., et al. Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation. Ann Neurol 42 326-334 (1997).

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