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Product Name
Nitrotyrosine
Catalog #
SMC-154D
Alternative Names
N/A
Clone Number
39B6
Immunogen
Hybridoma line 39B6
Accession Number
N/A
SwissProt
N/A
Applications
WB, ELISA, IHC, IP
Host Species
Mouse
Isotype
IgG2a
Species Reactivity
Human, Mouse, Rat, Dog
Recommended Dilutions
0.7μg/ml was sufficient for detection of 5µg SIN-1 treated BSA by Western Blot
Form
Protein G purified
Storage Buffer
PBS, 50% glycerol
Concentration
1mg/mL
Background Info
Recognizes 3-nitrotyrosine moieties. No detectable cross-reactivity with non-nitrated tyrosine. Not species specific.
Conjugate
N/A
Package Size
100ug
Storage Temp
-20°C
Shipping Temp
Blue Ice or 4°C
Datasheet
SMC 154 Nitrotyrosine Cell Signaling
Research Area
Cell Signaling, Oxidative Stress, Post-translational Modifications
Certificate of Analysis
0.7μg/ml of SMC-154 was sufficient for detection of 5μg SIN-1 treated BSA by Western Blot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Price
$297.00 USD Add to Cart

Nitrotyrosine visualized using SMC-154, tested in rat liver tissues.


Nitrotyrosine visualized using SMC-154, tested on Bouin's fixed paraffin-embedded backskin sections of transgenic mice.
Courtesy of Dr. Turksen, Ottawa Hospital Research Institute, Canada.
Research Background
Protein tyrosine nitration results in a post-translational modification that is increasingly receiving attention as an important component of nitric oxide signaling (2). While multiple nonenzymatic mechanisms are known to be capable of producing nitrated tyrosine residues, most tyrosine nitration events involve catalysis by metalloproteins such as myeloperoxidase, eosino-philperoxidase (3), myoglobin, the cytochrome P-450s, superoxide dismutase and prostacyclin synthase. Nitrotyrosine may also serve as a biomarker for the effects of reactive nitrogen oxides, based on tyrosine residues becoming nitrated in proteins at sites of inflammation induced tissue injury (1). The presence of nitro tyrosine-containing proteins therefore has shown high correlation to disease states such as atherosclerosis, Alzheimer’s disease, Parkinson’s disease and amyotrophic lateral sclerosis (4).
References
1. Girault I. et al. (2001). Free Radical Biology and Medicine, 31 (11): 1375-1387.
2. Gow AJ, Farkouh CR, Munson DA, Posencheq MA, and Ischiropoulos H. (2004). Am J Physiol Lung Cell Mol Physiol. 287(2): L262-8.
3. Takemoto K. et al (2007). Acta Med Okayama 61(1): 17-30.
4. Reynolds MR. et al. (2006) J Nerosci. 26(42): 10636-45.
5. Pfister H., et al. (2002) Vet Pathol. 39: 190-199.
6. Khan J. et al. (1998) Biochem J. 330(2): 795-801.
Cited References
Hyun-Seok Kim, Krish Patel, Kristi Muldoon-Jacobs, Kheem S. Bisht, Nukhet Aykin-Burns, J. Daniel Pennington, Riet van der Meer, Phuongmai Nguyen, Jason Savage, Kjerstin M. Owens, Athanassios Vassilopoulos, Ozkan Ozden, Seong-Hoon Park, Keshav K. Singh, Sarki A. Abdulkadir, Douglas R. Spitz, Chu-Xia Dengsend email, David Giuss. Cancer Cell, Volume 17, Issue 1, 41-52, 19 January 2010
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