Anti-AGE Antibody, Carboxy-Methyl Lysine Antibody, clone 6C7 clone 6C7, from mouse

Chronic accumulation of Advanced Glycation End products (AGEs) is a common feature during aging, hyperlipidemia, and diabetes and affects function of proteins, lipids, and DNA. Although formation of AGE products is considered to be predominantly an endogenous process, certain external factors, such as some dietary products and smoking can increase the level of AGE in tissues. Under certain conditions glucose may form covalent adducts with the plasma proteins through the process of glycation. Glycation is a non-enzymatic reaction of reducing carbohydrates with lysine side chains and N-terminal amino groups of proteins. The term AGE often refers to non-reactive terminal products, such as N- carboxymethyllysine (CML) as well as reactive precursors, such as methylglyoxal (MG). CML is an AGE product that is usually found on proteins and lipids as a result of oxidative stress and chemical glycation. Excessive glycation can disrupt protein function by altering enzyme activity, receptor function, and molecular conformation. Protein glycation and subsequent formation of AGE products contributes to the pathogenesis of diabetes-related complications, such as retinopathy, nephropathy, and neuropathy. Higher levels of CML have been linked to greater hip fracture risk in older adults, independent of bone mineral density. AGE products interact with a variety of cell-surface AGE-binding receptors (RAGE) that results in their endocytosis and degradation. It can also generate pro-oxidant and pro-inflammatory events in cells. AGE products could also contribute to the development or worsening of many degenerative diseases, including Alzheimer's disease. (Ref.: Cai, W., et al. (2002). Mol. Med 8 (7): 337-346; Barzilay, JI et al (2014). J. Bone Miner. Res. 29(5):1061-1066).