Goat Anti-MDA (Malondialdehyde) Affinity Pure | ABMC-A16
- SKU:
- ABMC-A16
- Availability:
- Usually shipped in 5 working days
Description
Goat Anti-MDA (Malondialdehyde) Affinity Pure | ABMC-A16
| Host Species: | Goat |
| 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 & 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).
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