CircuLex CEL-BSA /Nε-(Carboxyethyl)lysine-BSA

ELISA - 200-800 ng/ml

Reducing sugars react with protein amino groups to form a diverse group of protein-bound moieties with fluorescent and cross-linking properties. These compounds, called advanced glycosylation end products (AGEs), have been implicated in the structural and functional alterations of proteins that occur during aging and long-term diabetes. Although several AGE structures have been reported (1, 2), Nε-(Carboxymethyl) lysine (CML) and Nε-(carboxyethyl)lysine (CEL) stable, nonenzymatic chemical modifications of protein lysine residues resulting from glycation and oxidation reactions. CEL is a homologue of CML that is formed by the reaction of lysine residues in proteins with methylglyoxal as well as with triose phosphates and other sugars (3). CML and CEL are two major nonenzymatic chemical modifications on tissue proteins that can serve as biomarkers of oxidative stress resulting from sugar and lipid oxidation. CEL was detected in human skin collagen at 5?10% of the concentration detected in lens proteins from donors of similar age, and its concentration was approx. 8-fold higher in a pool of skin collagen samples from old, compared with young, donors (3). These observations suggest that CEL, like CML, will be a useful biomarker of the chemical aging of tissue proteins (4, 5).

1.0 mg/mL

The CE L-BSA /Nε-(carboxyethyl) lysine-BSA is supplied frozen in a buffer containing 10 mM PBS (pH 7.2).

Human: 1056 Mouse: 12613

1 year