CircuLex Glyceraldehyde-AGE-BSA

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) are two stable, nonenzymatic chemical modifications of protein lysine residues resulting from glycation and oxidation reactions. However it has been proposed that AGE are not only created from glucose per se, but also from dicarbonyl compounds derived from glycation, sugar autoxidation, and sugar metabolism. Various types of AGE, non-enzymatically glycated protein derivatives formed at an accelerated rate in diabetes (3), have been demonstrated to inhibit DNA synthesis and also induce apoptotic cell death in human mesangial cells (4).

1.0 mg/mL

The glyceraldehyde-AGE-BSA is supplied frozen in a buffer containing 10 mM PBS (pH 7.2).

1 year

Glyceraldehyde-AGE-BSA