[P21] Malondialdehyde modified Human ApoB-100 (MDA - ApoB-100), 50% glycerol - AcademyBiomed

[P21] Malondialdehyde modified Human ApoB-100 (MDA - ApoB-100), 50% glycerol


Academy Bio-Medical Company, Inc.

  • $269.00

Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Source: From fresh human plasma that has tested negative for Hepatitis C, HIV-I and HIV-II antibodies as well as Hepatitis surface antigens.
Purification: After ultracentrifugations, Low Density Lipoprotein (LDL) is isolated from human plasma. Water-soluble Apo B-100 is prepared from delipidated LDL(1), and modified with MDA.
Purity: LDL as starting material containing 98% of apoB-100.
Buffer: 75 mM PBS, 75 mM NaCl, pH 7.4, 0.5 mM EDTA, 0.02 % NaN3. Preserved with 50% glycerol.
Storage: -20ºC for long-term and short-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



[P21] 2012 Kamath, Amrita V.; Williams, Simon P.; Bullens, Sherry; Cowan, Kyra J.; Stenberg, Yvonne; Cherry, Simon R. et al. (2012): Pharmacokinetics and biodistribution of a human monoclonal antibody to oxidized LDL in cynomolgus monkey using PET imaging. In PLoS ONE 7 (9), e45116. DOI: 10.1371/journal.pone.0045116.
[P21] 2007 Ström, Asa; Fredrikson, Gunilla Nordin; Schiopu, Alexandru; Ljungcrantz, Irena; Söderberg, Ingrid; Jansson, Bo et al. (2007): Inhibition of injury-induced arterial remodelling and carotid atherosclerosis by recombinant human antibodies against aldehyde-modified apoB-100. In Atherosclerosis 190 (2), pp. 298–305. DOI: 10.1016/j.atherosclerosis.2006.03.032.
[P21] 2004 Schiopu, Alexandru; Bengtsson, Jenny; Söderberg, Ingrid; Janciauskiene, Sabina; Lindgren, Stefan; Ares, Mikko P. S. et al. (2004): Recombinant human antibodies against aldehyde-modified apolipoprotein B-100 peptide sequences inhibit atherosclerosis. In Circulation 110 (14), pp. 2047–2052. DOI: 10.1161/01.CIR.0000143162.56057.B5.


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