[P24] Malondialdehyde modified Bovine Serum Albumin (MDA - BSA), 50% glycerol20P-MD-BS102
|Concentration:||1 mg / ml, determined by the Lowry method|
|Source:||Bovine Serum Albumin purchased from Boehringer Mannheim and modified with MDA.|
|Buffer:||In 10 mM PBS, 0.15 M NaCl 0.5 mM EDTA, 0.01 % NaN3. In addition, preserved with 50 % glycerol.|
|Storage:||-20°C for short and long-term storage. Aliquot to avoid repeated freezing and thawing.|
*The products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.
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
|[P24]||2018||Hardt, Uta; Larsson, Anders; Gunnarsson, Iva; Clancy, Robert M.; Petri, Michelle; Buyon, Jill P. et al. (2018): Autoimmune reactivity to malondialdehyde adducts in systemic lupus erythematosus is associated with disease activity and nephritis. In Arthritis research & therapy 20 (1), p. 1878. DOI: 10.1186/s13075-018-1530-2.|
|[P24]||2018||Pujol-Lereis, Luciana M.; Liebisch, Gerhard; Schick, Tina; Lin, Yuchen; Grassmann, Felix; Uchida, Koji et al. (2018): Evaluation of serum sphingolipids and the influence of genetic risk factors in age-related macular degeneration. In PLoS ONE 13 (8), e0200739. DOI: 10.1371/journal.pone.0200739.|
|[P24]||2017||Grönwall, Caroline; Amara, Khaled; Hardt, Uta; Krishnamurthy, Akilan; Steen, Johanna; Engström, Marianne et al. (2017): Autoreactivity to malondialdehyde-modifications in rheumatoid arthritis is linked to disease activity and synovial pathogenesis. In Journal of autoimmunity 84, pp. 29–45. DOI: 10.1016/j.jaut.2017.06.004.|
|[P24]||2017||Grönwall, Caroline; Hardt, Uta; Gustafsson, Johanna T.; Elvin, Kerstin; Jensen-Urstad, Kerstin; Kvarnström, Marika et al. (2017): Depressed serum IgM levels in SLE are restricted to defined subgroups. In Clinical Immunology 183, pp. 304–315. DOI: 10.1016/j.clim.2017.09.013.|
|[P24]||2016||Grönwall, Caroline; Clancy, Robert M.; Getu, Lelise; Lloyd, Katy A.; Siegel, Don L.; Reed, Joanne H. et al. (2016): Modulation of natural IgM autoantibodies to oxidative stress-related neo-epitopes on apoptotic cells in newborns of mothers with anti-Ro autoimmunity. In Journal of autoimmunity 73, pp. 30–41. DOI: 10.1016/j.jaut.2016.05.014.|
|[P24]||2016||Rother, Magdalena B.; Schreurs, Marco W. J.; Kroek, Roel; Bartol, Sophinus J. W.; van Dongen, Jacques J. M.; van Zelm, Menno C. (2016): The Human Thymus Is Enriched for Autoreactive B Cells. In J. Exp. Med. 197 (2), pp. 441–448. DOI: 10.4049/jimmunol.1501992.|
|[P24]||2014||Grönwall, Caroline; Charles, Edgar D.; Dustin, Lynn B.; Rader, Christoph; Silverman, Gregg J. (2014): Selection of apoptotic cell specific human antibodies from adult bone marrow. In PLoS ONE 9 (4), e95999. DOI: 10.1371/journal.pone.0095999.|
|[P24]||2014||Schwartz, Marc A.; Kolhatkar, Nikita S.; Thouvenel, Chris; Khim, Socheath; Rawlings, David J. (2014): CD4+ T cells and CD40 participate in selection and homeostasis of peripheral B cells. In J.I. 193 (7), pp. 3492–3502. DOI: 10.4049/jimmunol.1400798.|
|[P24]||2009||Chen, Yifang; Park, Yong-Beom; Patel, Ekta; Silverman, Gregg J. (2009): IgM antibodies to apoptosis-associated determinants recruit C1q and enhance dendritic cell phagocytosis of apoptotic cells. In J.I. 182 (10), pp. 6031–6043. DOI: 10.4049/jimmunol.0804191.|