CEL (N-Epsilon)-Carboxyethyl-LysineCatalogue number: CEL025
This antibody is suitable for the detection of CEL in tissues and tissue extracts. Long-term incubation of proteins with glucose leads, through Schiff's base and Amadori rearrangement products, to the formation of advanced glycation end products (AGE) which are characterized by fluorescence, brown color and inter- and intra-molecular cross-linking. Recent immunological studies using anti-AGE antibodies demonstrated the presence of AGE in (i) human lens, (ii) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure, (iii) atherosclerotic lesions of arterial walls, (iv) ß2-microglobulin of carpal tunnel amyloid fibril deposits in patients with hemodialysis-related amyloidosis and (v) brain tissues of patients with Alzheimer’s disease. According to McLellan et al. (1994) CEL is formed as a reaction product of methylglyoxal (MG) with proteins in diabetes patients. In these patiens up to 7 times higher MG-values were measured in comparison to healthy subjects. In lenses of diabetic patients CEL concentration was found to be as high as that of CML [N-epsilon-(carboxymethyl)lysine].
Protein G affinity purified antibody from ascites in stabilized buffer, PBS + 2% Block ACE and 0,1% Proclin as a bacteriostat
Purification Method: Protein G affinity purified antibody from ascites in stabilized buffer, containing 50% Block Ace? (Casein-containing solution, Dainippon Co.) and 0.1% ProClin? (Rohm & Haas) as a preservative
Concentration: 0.25 mg/ml
Secondary Reagents: We recommend the use of BIOLOGO's Universal Staining System DAB (Art. No. DA005) or AEC (Art. No. AE005).
Incubation Time: 60 min at RT or 18 hr at 2-8°C
Working Concentration: (liquid conc.) ELISA 0.1-0.5 µg/ml; IHC 2 µg/ml
Positive Control: Diabetic lens cataract
These antibodies are intended for in vitro research use only. They must not be used for clinical diagnostics and not for in vivo experiments in humans or animals.
1. Horiuchi S., Araki N., and Morino Y. (1991) Immunological approach to characterize advanced glycation end products of the Maillard reaction: Evidence for the presence of a common stucture. J. Biol. Chem. 266; 7329-7332. 2. McLellan AC, Thornalley PJ, Benn J, Sonksen PH (1994) Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clinical Science 87: 21-29. 3. Ahmed MU, Brinkmann E, Degenhardt TP, Thorpe SR, Baynes JW (1997) Ne-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem J 324:565-570. 4. Degenhardt TP, Thorpe SR, Baynes JW (1998) Chemical modification of proteins by methylglyoxal. Cell Mol Biol 44:1139-1145.