Nitrotyrosine Antikörper

Produktnummer ABIN361658

Dieses Maus Monoklonal-Antikörper erkennt spezifisch Nitrotyrosine in WB, ELISA, IP, IHC, FACS, ICC, IF und AA. Er zeigt eine Reaktivität gegenüber und wurde in 9+ Publikationen erwähnt.

Kurzübersicht für Nitrotyrosine Antikörper (ABIN361658)

Target: Nitrotyrosine

Reaktivität: Bitte anfragen

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser Nitrotyrosine Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunohistochemistry (IHC), Flow Cytometry (FACS), Immunocytochemistry (ICC), Immunofluorescence (IF), Antibody Array (AA)

Klon: 39B6

Produktdetails anti-Nitrotyrosine Antikörper

Spezifität: Recognizes 3-nitrotyrosine moieties. No detectable cross-reactivity with non-nitrated tyrosine. Not species specific.

Aufreinigung: Protein G Purified

Immunogen: 3-(4-hydroxy-3-nitrophenylacetamido) propionic acid-bovine serum albumin

Isotyp: IgG2a

Anwendungsinformationen

Applikationshinweise:

• WB (1:1400)
• IHC (1:100)
• optimal dilutions for assays should be determined by the user.

Kommentare:

0.7 μg/ml of ABIN361657 was sufficient for detection of 5 μg SIN-1 treated BSA by Western Blot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 1 mg/mL

Buffer: PBS, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: -20 °C

Informationen zur Lagerung: -20°C

Referenzen für anti-Nitrotyrosine Antikörper (ABIN361658)

Wert, Velez, Cross, Wagner, Teoh-Fitzgerald, Buettner, McAnany, Olivier, Tsang, Harper, Domann, Bassuk, Mahajan: "Extracellular superoxide dismutase (SOD3) regulates oxidative stress at the vitreoretinal interface." in: Free radical biology & medicine, Vol. 124, pp. 408-419, (2019) (PubMed).

Matsui, Nakashima, Nishino, Ojima, Nakamura, Arima, Fukami, Okuda, Yamagishi: "Dipeptidyl peptidase-4 deficiency protects against experimental diabetic nephropathy partly by blocking the advanced glycation end products-receptor axis." in: Laboratory investigation; a journal of technical methods and pathology, Vol. 95, Issue 5, pp. 525-33, (2015) (PubMed).

Takikawa, Nakamura, Ishihara, Takabayashi, Fujita, Hattori, Kushibiki, Ishihara: "Improved angiogenesis and healing in crush syndrome by fibroblast growth factor-2-containing low-molecular-weight heparin (Fragmin)/protamine nanoparticles." in: The Journal of surgical research, Vol. 196, Issue 2, pp. 247-57, (2015) (PubMed).

Nakajima, Kubo, Ihara, Hikida, Danjo, Nakatsuji, Shahani, Itakura, Ono, Azuma, Inui, Kamiya, Sawa, Takeuchi: "Nuclear-translocated Glyceraldehyde-3-phosphate Dehydrogenase Promotes Poly(ADP-ribose) Polymerase-1 Activation during Oxidative/Nitrosative Stress in Stroke." in: The Journal of biological chemistry, Vol. 290, Issue 23, pp. 14493-503, (2015) (PubMed).

Ampem, Azegrouz, Bacsadi, Balogh, Schmidt, Thuróczy, Röszer: "Adipose tissue macrophages in non-rodent mammals: a comparative study." in: Cell and tissue research, (2015) (PubMed).

Nakayama, Fujita, Ishihara, Ishihara, Ogata, Yamamoto, Shimizu, Maehara, Kanatani, Tachibana: "Improved survival rate by temperature control at compression sites in rat model of crush syndrome." in: The Journal of surgical research, Vol. 188, Issue 1, pp. 250-9, (2014) (PubMed).

Chao, Chang, Su, Su: "Inducible nitric oxide synthase mediates MG132 lethality in leukemic cells through mitochondrial depolarization." in: Free radical biology & medicine, Vol. 74, pp. 175-87, (2014) (PubMed).

Grutzmacher, Park, Zhao, Morrison, Sheibani, Sorenson: "Aberrant production of extracellular matrix proteins and dysfunction in kidney endothelial cells with a short duration of diabetes." in: American journal of physiology. Renal physiology, Vol. 304, Issue 1, pp. F19-30, (2013) (PubMed).

Kim, Patel, Muldoon-Jacobs, Bisht, Aykin-Burns, Pennington, van der Meer, Nguyen, Savage, Owens, Vassilopoulos, Ozden, Park, Singh, Abdulkadir, Spitz, Deng, Gius: "SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress." in: Cancer cell, Vol. 17, Issue 1, pp. 41-52, (2010) (PubMed).

Details zu Nitrotyrosine

Target: Nitrotyrosine

Substanzklasse: Chemical

Hintergrund: 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).