Polyclonal Anti- Advanced Glycated End-products (AGE) Antiserum 

Glycation is a post-translational modification of proteins involving a covalent linkage between a reducing sugar, such as glucose, and a receptive amino group via the non-enzymatic Maillard reaction.  During the early stages of the Maillard reaction, the aldehyde groups of the reducing sugars react with the amino groups of N-terminal amino acids to form Schiff bases, which are then converted to Amadori compounds.  In the advanced stages, these Amadori compounds undergo oxidation, dehydration and condensation to form advanced glycation end-products (AGE) that are characterized by fluorescence, browning, and intra- or inter-molecular cross-linking properties. The main AGE products are pentosine and carboxymethyllysine (CML).

Pentosidine is a main AGE compound that is formed from cross-linked lysine and arginine residues of proteins and reducing sugars.  Pentosine is a stable AGE-structure and its levels increase in aging, diabetes, cataracts, renal diseases, chronic rheumatoid arthritis, photoaged skin and in brain lesions associated with Alzheimer’s disease.  CML is formed by the irreversible oxidation of Amodori products and is the major non-fluorescent AGE in uracemia.  AGE formation is especially predominant under conditions of high sugar concentrations, such as diabetes.  AGEs are thought to play an important role in the structural and functional alterations that occur in proteins during long-term aging and diabetes such as blindness, renal failure, neuropathy and vascular disease.

It is known that glycoaldehyde is an efficient precursor of CML.  Glycoaldehyde modified proteins have also been shown to contain high levels of pentosine formation¸suggesting that glycoaldehyde is a potent precursor of pentosine.  Therefore, glycoaldehyde-modified proteins contain both pentosine and CML epitopes.  Antibodies raised to glycoaldehyde-modified proteins have been shown to detect AGE-modified proteins as well as both pentosine-modifed BSA and CML-modified BSA.

A goat anti-AGE antiserum produced using a glycoaldehyde-modified protein is currently available. This antiserum has been shown to be immunoreactive with glycoaldehyde-modified BSA by ELISA and detects AGE-modified proteins on western blots. This antibody should be a valuable tool for scientists working to understand the role of AGE in diabetes, aging and other neurological diseases.

Glycoaldehyde-modified bovine serum albumin is available (Cat No. HMP036H), which can be used to neutralize immunoreactivity.

Manufacturing Reference:

Farboud, B., Aotaki-Keen, A., Miyata, T., et al.  Mol. Vis. 1999; 5:11 (www.molvis.org/molvis/v5/p11).