Protein Carbonyl Immunoblot Kit

  • DNPH derivatization after blotting allows direct comparison of oxidized and non-oxidized protein fingerprints
  • Suitable for plasma, serum, cell lysates or purified proteins


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OxiSelect™ Protein Carbonyl Immunoblot Kit
Catalog Number
10 blots
Manual/Data Sheet Download
SDS Download
OxiSelect™ Protein Carbonyl Immunoblot Kit, Trial Size
Catalog Number
4 blots
Manual/Data Sheet Download
SDS Download
Product Details

The most common products of protein oxidation in biological samples are the carbonyl derivatives of proline, lysine, arginine and threonine residues. Such derivatives are chemically stable and serve as markers for oxidative stress in most types of reactive oxygen species.

Our OxiSelect™ Protein Carbonyl Immunoblot Kit provides a rapid, efficient method for the detection of protein carbonyl residues. The immunoblot format provides a convenient way to compare oxidized and non-oxidized protein fingerprints.

Assay Principle for the OxiSelect™ Protein Oxidation Immunoblot Kit.

Recent Product Citations
  1. Galmes-Pascual, B.M. et al. (2016). 17ß-estradiol improves hepatic mitochondrial biogenesis and function through PGC1B. J. Endocrinol. 232:297-308.
  2. Su, L. et al. (2016). Reactive oxygen species induced by cold stratification promote germination of Hedysarum scoparium seeds. Plant Physiol. Biochem. 109:406-415.
  3. Ferrer, M.D. et al. (2016). Haem biosynthesis and antioxidant enzymes in circulating cells of acute intermittent porphyria patients. PLoS One doi:10.1371/journal.pone.0164857.
  4. Capo, X. et al. (2016). Effects of dietary almond-and olive oil-based docosahexaenoic- and vitamin E-enriched beverage supplementation on athletic performance and oxidative stress. Food Funct. 7:4920-4934.
  5. Chaves, R. S. et al. (2016). Presence of insoluble Tau following rotenone exposure ameliorates basic pathways associated with neurodegeneration. IBRO Rep. doi:10.1016/j.ibror.2016.09.001.
  6. Almeida, M. F. et al.. Aged Lewis rats exposed to low and moderate doses of rotenone are a good model for studying the process of protein aggregation and its effects upon central nervous system cell physiology. Arq Neuropsiquiatr74:737-744.
  7. Ong, L. K. et al. (2016). Reconsidering the role of glial cells in chronic stress-induced dopaminergic neurons loss within the substantia nigra? Friend or foe?. Brain Behav Immun.  doi:10.1016/j.bbi.2016.10.001.
  8. Busquets-Cortés, C. et al. (2016). Training enhances immune cells mitochondrial biosynthesis, fission, fusion, and their antioxidant capabilities synergistically with dietary docosahexaenoic supplementation. Oxid Med Cell Longev. doi:10.1155/2016/8950384.
  9. Hudgens, J. L. et al. (2016). Platelet-rich plasma activates proinflammatory signaling pathways and induces oxidative stress in tendon fibroblasts. Am J Sports Med. doi:10.1177/0363546516637176.
  10. Laitano, O. et al. (2016). Pharmacological targeting of mitochondrial reactive oxygen species counteracts diaphragm weakness in chronic heart failure. J Appl Physiol. doi:10.1152/japplphysiol.00822.2015.
  11. Tanase, M. et al. (2016). Role of carbonyl modifications on aging-associated protein aggregation. Sci Rep. doi:10.1038/srep19311.
  12. ElHajj, Z. et al. (2016). Effects of postmortem delays on protein composition and oxidation. Brain Res Bull. doi:10.1016/j.brainresbull.2016.01.005.
  13. Sbert-Roig, M. et al. (2015). GPER mediates the effects of 17β-estradiol in cardiac mitochondrial biogenesis and function. Mol Cell Endocrinol. doi:10.1016/j.mce.2015.11.027.
  14. Zhou, J. et al. (2015). Correlations between photodegradation of bisretinoid constituents of retina and dicarbonyl adduct deposition. J Biol Chem.290:27215-27227.
  15. Martorell, M. et al. (2015). Docosahexaenoic acid supplementation promotes erythrocyte antioxidant defense and reduces protein nitrosative damage in male athletes. Lipids. 50:131-148.
  16. Capó, X. et al. (2015). Diet supplementation with DHA-enriched food in football players during training season enhances the mitochondrial antioxidant capabilities in blood mononuclear cells. Eur J Nutr. 54:35-49.
  17. Cui, J. et al. (2015). Rapamycin protects against gentamicin-induced acute kidney injury via autophagy in mini-pig models. Sci Rep. doi:10.1038/srep11256.
  18. Konopka, A. R. et al. (2015). Defects in mitochondrial efficiency and H2O2 emissions in obese women are restored to a lean phenotype with aerobic exercise training. Diabetes. 64:2104-2115.
  19. Pons, D. G. et al.  (2015). UCP2 inhibition sensitizes breast cancer cells to therapeutic agents by increasing oxidative stress. Free Radic Biol Med.  doi:10.1016/j.freeradbiomed.2015.04.032.
  20. Nadal-Serrano, M. et al. (2015). Chronic-leptin attenuates cisplatin cytotoxicity in MCF-7 breast cancer cell line. Cell Physiol Biochem. 36:221-232.
  21. Blanquer-Rossello, M. D. et al. (2015). Leptin modulates mitochondrial function, dynamics and biogenesis in MCF-7 cells. J Cell Biochem. doi: 10.1002/jcb.25158.
  22. Cao, W. et al. (2015). Geranylgeranylacetone ameliorates lung ischemia/reperfusion injury by HSP70 and thioredoxin redox system: NF-kB pathway involved. Pulm Pharmacol Ther. doi: 10.1016/j.pupt.2015.02.009. 
  23. Konopka, A. R. et al. (2015). Defects in mitochondrial efficiency and H2O2 emissions in obese women are restored to a lean phenotype with aerobic exercise training. Diabetes.doi: 10.2337/db14-1701.
  24. Martorell, M. et al. (2014). Docosahexaenoic acid supplementation promotes erythrocyte antioxidant defense and reduces protein nitrosative damage in male athletes. Lipids. 50:131-148.
  25. Wang, Z. H. et al. (2014). Concentration-dependent wrestling between detrimental and protective effects of H2O2 during myocardial ischemia/reperfusion. Cell Death Dis. 5:e1297.
  26. Chen, C. et al. (2014). C75, An inhibitor of fatty acid synthase, suppresses the mitochondrial fatty acid synthesis pathway and impairs mitochondrial function. J Biol Chem. 289:17184-17194.
  27. Hwee, D. T. et al. (2014). Maintenance of muscle mass and load‐induced growth in Muscle RING Finger 1 null mice with age. Aging Cell.  13:92-101.
  28. Galay, R. L. et al. (2014). Two kinds of ferritin protect ixodid ticks from iron overload and consequent oxidative stress. PLoS One. 9:e90661.
  29. Cao, K. et al. (2014). AMPK activation prevents prenatal stress-induced cognitive impairment: Modulation of mitochondrial content and oxidative stress. Free Radic Biol Med. 75:156-166.
  30. Cao, K. et al. (2014). Hydroxytyrosol prevents diet-induced metabolic syndrome and attenuates mitochondrial abnormalities in obese mice. Free Radic Biol Med. 67:396-407.
  31. Enzor, L. A. and Place, S. P. (2014).  Is Warmer Better? Decreased Oxidative Damage in Notothenioid Fish After Long-Term Acclimation to Multiple Stressors. J Exp Biol. 217:3301-3310.
  32. Chen, C. et al. (2014).  4-Methylene-2-octyl-5-oxotetrahydrofuran-3-carboxylic Acid (C75), an Inhibitor of Fatty-acid Synthase, Suppresses the Mitochondrial Fatty Acid Synthesis Pathway and Impairs Mitochondrial Function. J Biol Chem. 289:17184-17194.
  33. Capllonch-Amer, G. et al. (2014).  Estradiol Stimulates Mitochondrial Biogenesis and Adiponectin Expression in Skeletal Muscle. J Endocrinol. 221:391-403.
  34. Xu, J. et al. (2014). Bitter gourd inhibits the development of obesity-associated fatty liver in C57BL/6 mice fed a high-fat diet. J. Nutr. 144:475-483.
  35. Cui, Z. et al. (2014). Identification of the Immunoproteasome as a Novel Regulator of Skeletal Muscle Differentiation. Mol. Cell. Biol. 34:96-109.
  36. Pons, D. et al. (2012). Initial Activation Status of the Antioxidant Response Determines Sensitivity to Carboplatin/Paclitaxel Treatment of Ovarian Cancer. Anticancer Res. 32:4723-4728.
  37. Cristovao, A.C. et al. (2012). NADPH Oxidase 1 Mediates α-Synucleinopathy in Parkinson's Disease. J. Neurosci. 32: 14465-14477.
  38. Bitar, M. et al. (2012).Decline in DJ-1 and Decreased Nuclear Translocation of Nrf2 in Fuchs Endothelial Corneal Dystrophy. Invest. Opthalmol. Vis. Sci. 53:5806-5813.
  39. Satapati, S. et al. (2012). Elevated TCA Cycle Function in the Pathology of Diet-Induced Hepatic Insulin Resistance and Fatty Liver. J.Lipid Res. 53:1080-1092.
  40. Bradshaw, A. et al. (2011). Cross-linking by Protein Oxidation in the Rapidly Setting Gel-based Glues of Slugs. J. Exp. Biol. 214:1699-1706.
  41. Snider, N.T. et al. (2011). Energy Determinants GAPDH and NDPK Act as Genetic Modifiers for Hepatocyte Inclusion Formation. J. Cell Biol. 195:217-229.
  42. Maity, P. et al. (2008). Indomethacin, a Non-Steroidal Anti-Inflammatory Drug, Develops Gastropathy by Inducing Reactive Oxygen Species-Mediated Mitochondrial Pathology and Associated Apoptosis in Gastric Mucosa: A Novel Role of Mitochondrial Aconitase Oxidation. J. Biol. Chem. 284:3058-3068.
  43. Jia, L. et al. (2007). Acrolein, a Toxicant in Cigarette Smoke, causes Oxidative Damage and Mitochondrial Dysfunction in RPE Cells: Protection by (R)-Alpha-Lipoic Acid. Invest. Ophthalmol. Vis. Sci. 48:339-348.
  44. Liu, Z. et al. (2007). Hydroxytyrosol Protects Retinal Pigment Epithelia lCells from Acrolein-Induced Oxidative Stress and Mitochondrial Dysfunction. J. Neurochem. 103:2690-2700.