[A17] Rabbit Anti-MDA (Malondialdehyde) Polyclonal Antibody, 30% glycerol

[A17] Rabbit Anti-MDA (Malondialdehyde) Polyclonal Antibody, 30% glycerol

MD20A-R1a

Academy Bio-Medical Company, Inc.

  • $441.00


Host Species: Rabbit
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: MDA-KLH
Purification: Affinity purified
Buffer: 75 mM Sodium Phosphate, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, pH 7.2
Specificity Specifically binds to MDA-LDL and other MDA modified proteins. Dilution for immunoblot and ELISA range: 1,000 to 20,000. (A slight amount of precipitation may have occurred during storage due to the natural properties of these antibodies; please centrifuge before use.)
Use: The antibody can be used for detection of MDA in plasma, lipoproteins and other MDA modified proteins, immunoassays, immunoblots, enzyme conjugation, or biotinylation.
Storage: -20°C for long-term storage, 4°C for short- term storage. Aliquot to avoid repeated freezing and thawing.

 

*These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.

Importance

Oxidative damage includes oxidative modification of cellular macromolecules, induction of cell death by apoptosis or necrosis, as well as structural tissue damage. Of the many biological targets of oxidative stress, lipids are the most involved class of biomolecules. Lipid oxidation gives rise to a number of secondary products of polyunsaturated fatty acid peroxidation. Malondialdehyde (MDA) is the principal and most studied product. Consistent evidence reveals the reaction between MDA and cellular macromolecules such as proteins, RNA and DNA (Valenzuela, 1991).

Numerous experiments have shown that MDA readily modifies proteins (Nair, 1986). MDA reacts with DNA to form adducts to deoxyguanosine and deoxyadenosine which may be mutagenic and these can be quantified in several human tissues (Marnett, 1999).This aldehyde is a highly toxic molecule and should be considered as a marker of lipid peroxidation. The interaction with DNA and proteins has often been referred to as potentially mutagenic and atherogenic (Rio et al., 2005).

L.J. Marnett, Lipid peroxidation‐DNA damage by malondialdehyde, Mutat Res, 424 (1999), pp. 83–95

V. Nair, C.S. Cooper, D.E. Vietti, G.A. Turner, The chemistry of lipid peroxidation metabolites: crosslinking reactions of malondialdehyde, Lipids, 21 (1986), pp. 6–10

Rio, Daniele Del, Amanda J. Stewart, and Nicoletta Pellegrini. "A Review of Recent Studies on Malondialdehyde as Toxic Molecule and Biological Marker of Oxidative Stress." Nutrition, Metabolism and Cardiovascular Diseases 15.4 (2005): 316-28.

A. Valenzuela, The biological significance of malondialdehyde determination in the assessment of tissue oxidative stress, Life Sci, 48 (1991), pp. 301–309

 

Citations

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[A16][A17] 2018 Barreiro, Esther; Puig-Vilanova, Ester; Salazar-Degracia, Anna; Pascual-Guardia, Sergi; Casadevall, Carme; Gea, Joaquim (2018): The phosphodiesterase-4 inhibitor roflumilast reverts proteolysis in skeletal muscle cells of patients with COPD cachexia. In Journal of Applied Physiology 125 (2), pp. 287–303. DOI: 10.1152/japplphysiol.00798.2017.
[A16][A17] 2018 Yamada, Ryotaro; Himori, Koichi; Tatebayashi, Daisuke; Ashida, Yuki; Ikezaki, Kazumi; Miyata, Hirohumi et al. (2018): Preconditioning contractions prevent the delayed onset of myofibrillar dysfunction after damaging eccentric contractions. In J Physiol 596 (18), pp. 4427–4442. DOI: 10.1113/JP276026.
[A16][A17] 2017 Salazar-Degracia, Anna; Busquets, Sílvia; Argilés, Josep M.; López-Soriano, Francisco J.; Barreiro, Esther (2017): Formoterol attenuates increased oxidative stress and myosin protein loss in respiratory and limb muscles of cancer cachectic rats. In PeerJ 5 (Suppl 1), e4109. DOI: 10.7717/peerj.4109.
[A16][A17] 2016 Salazar-Degracia, Anna; Blanco, David; Vilà-Ubach, Mònica; Biurrun, Gabriel de; Solórzano, Carlos Ortiz de; Montuenga, Luis M.; Barreiro, Esther (2016): Phenotypic and metabolic features of mouse diaphragm and gastrocnemius muscles in chronic lung carcinogenesis: influence of underlying emphysema. In Journal of translational medicine 14 (1), p. 244. DOI: 10.1186/s12967-016-1003-9.
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[A16][A17] 2014 Yang, Tzu-Ching; Chen, Yi-Jie; Chang, Shwu-Fen; Chen, Chu-Huang; Chang, Po-Yuan; Lu, Shao-Chun (2014): Malondialdehyde mediates oxidized LDL-induced coronary toxicity through the Akt-FGF2 pathway via DNA methylation. In Journal of biomedical science 21, p. 11. DOI: 10.1186/1423-0127-21-11.
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[A16][A17] 2013 Arashiki, Nobuto; Kimata, Naoki; Manno, Sumie; Mohandas, Narla; Takakuwa, Yuichi (2013): Membrane peroxidation and methemoglobin formation are both necessary for band 3 clustering: mechanistic insights into human erythrocyte senescence. In Biochemistry 52 (34), pp. 5760–5769. DOI: 10.1021/bi400405p.
[A16][A17] 2013 Serrano, José C. E.; Gonzalo-Benito, Hugo; Jové, Mariona; Fourcade, Stéphane; Cassanyé, Anna; Boada, Jordi et al. (2013): Dietary intake of green tea polyphenols regulates insulin sensitivity with an increase in AMP-activated protein kinase α content and changes in mitochondrial respiratory complexes. In Molecular nutrition & food research 57 (3), pp. 459–470. DOI: 10.1002/mnfr.201200513.
[A16][A17] 2013 van den Borst, Bram; Slot, Ilse G. M.; Hellwig, Valéry A. C. V.; Vosse, Bettine A. H.; Kelders, Marco C. J. M.; Barreiro, Esther et al. (2013): Loss of quadriceps muscle oxidative phenotype and decreased endurance in patients with mild-to-moderate COPD. In Journal of Applied Physiology 114 (9), pp. 1319–1328. DOI: 10.1152/japplphysiol.00508.2012.
[A16][A17] 2012 Barreiro, Esther; del Puerto-Nevado, Laura; Puig-Vilanova, Ester; Pérez-Rial, Sandra; Sánchez, Francisco; Martínez-Galán, Lourdes et al. (2012): Cigarette smoke-induced oxidative stress in skeletal muscles of mice. In Respiratory Physiology & Neurobiology 182 (1), pp. 9–17. DOI: 10.1016/j.resp.2012.02.001.
[A16][A17] 2012 Fukunaga, Naoya; Takahashi, Naohiko; Hagiwara, Satoshi; Kume, Osamu; Fukui, Akira; Teshima, Yasushi et al. (2012): Establishment of a model of atrial fibrillation associated with chronic kidney disease in rats and the role of oxidative stress. In Heart Rhythm 9 (12), pp. 2023–2031. DOI: 10.1016/j.hrthm.2012.08.019.
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[A16][A17] 2005 Pamplona, Reinald; Dalfó, Esther; Ayala, Victòria; Bellmunt, Maria Josep; Prat, Joan; Ferrer, Isidre; Portero-Otín, Manuel (2005): Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. In J. Biol. Chem. 280 (22), pp. 21522–21530. DOI: 10.1074/jbc.M502255200.
[A16][A17] 2005 Pamplona, Reinald; Portero-Otín, Manuel; Sanz, Alberto; Ayala, Victoria; Vasileva, Ekaterina; Barja, Gustavo (2005): Protein and lipid oxidative damage and complex I content are lower in the brain of budgerigar and canaries than in mice. Relation to aging rate. In Age (Dordrecht, Netherlands) 27 (4), pp. 267–280. DOI: 10.1007/s11357-005-4562-x.
[A16][A17] 2005 Yarian, Connie S.; Rebrin, Igor; Sohal, Rajindar S. (2005): Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria. In Biochemical and biophysical research communications 330 (1), pp. 151–156. DOI: 10.1016/j.bbrc.2005.02.135.
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[A16][A17] 2004 Ye, Gang; Metreveli, Naira S.; Donthi, Rajakumar V.; Xia, Shen; Xu, Ming; Carlson, Edward C.; Epstein, Paul N. (2004): Catalase protects cardiomyocyte function in models of type 1 and type 2 diabetes. In Diabetes 53 (5), pp. 1336–1343. DOI: 10.2337/diabetes.53.5.1336.

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