ALEXIS Biochemicals: Monoclonal Antibody to Nitrotyrosine (CC22.8C7)

ALX-804-204

Revised 07-Oct-08

Monoclonal Antibody to Nitrotyrosine (CC22.8C7)
PRODUCT LINE	Nitric Oxide Pathway
PRODUCT CATEGORY	Nitrotyrosine / Related Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-804-204-C050		50 µg	126.00 USD
ALX-804-204B-C100	Biotin	100 µg	357.00 USD
ALX-804-204-C200		200 µg	448.00 USD

Product Specification

CLONE:	CC22.8C7
ISOTYPE:	Mouse IgG2b
CONCENTRATION:
FORMULATION:	CC22.8C7: Liquid. In PBS, pH 7.2, containing 50% glycerol, 0.1mg/ml BSA and 0.02% sodium azide. CC22.8C7-Biotin: Liquid. In PBS, pH 7.2, containing 0.5mg/ml BSA and 0.02% sodium azide.
IMMUNOGEN:	Peroxynitrite-treated KLH (keyhole limpet hemocyanin).
SPECIFICITY:	Recognizes nitrotyrosine-containing proteins.
APPLICATION:	ELISA [1] Immunohistochemistry (10µg/ml) Immunoprecipitation Western Blot (1-2µg/ml) Optimal conditions must be determined individually for each application.
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C
USE/STABILITY:	CC22.8C7: Stable for at least 2 years after receipt when stored at -20°C. CC22.8C7-Biotin: Stable for at least 1 year after receipt when stored at +4°C.
POSITIVE CONTROL:	For Positive Control see Prod. No. ALX-840-013.

Product Specific Literature References

[1] Enzyme immunoassays for the investigation of protein nitration by air pollutants: T. Franze, et al.; Analyst. 128, 824 (2003) Abstract

General Information

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/sec) 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. Nitrotyrosine has been shown to be present in proteins from a variety of clinical conditions including atherosclerotic lesions of human coronary arteries, postischemic heart, and placenta during preeclampsia. 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.

General Literature References

Oxidative chemistry of peroxynitrite: J.S. Beckman, et al.; Meth. Enzymol. 233, 229 (1994) Abstract
Extensive nitration of protein tyrosines in human atherosclerosis detected by immunohistochemistry: J.S. Beckman, et al.; Biol. Chem. Hoppe-Seyler 375, 81 (1994) Abstract
Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and the ugly: J.S. Beckman and W.H. Koppenol; Am. J. Physiol. 271, C1424 (1996) Abstract
Measurement of nitric oxide and peroxynitrite generation in the postischemic heart. Evidence for peroxynitrite-mediated reperfusion injury: P. Wang and J.L. Zweier; J. Biol. Chem. 271, 29223 (1996) Abstract; Full Text
Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amytrophic lateral sclerosis: An immunohistochemical study: S.M. Chou, et al.; J. Chem. Neuroanat. 10, 249 (1996) Abstract
Nitrotyrosine residues in placenta. Evidence of peroxynitrite formation and action: L. Myatt, et al.; Hypertension 28, 488 (1996) Abstract
Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation: R.J. Ferrante, et al.; Ann. Neurol. 42, 326 (1997) Abstract
Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis: K. Abe, et al.; Neurol. Res. 19, 124 (1997) Abstract

Further Categories Containing This Product:

Monoclonal Antibodies

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