English
CEL (N-Epsilon)-Carboxyethyl-Lysine
CEL (N-Epsilon)-Carboxyethyl-Lysine, IgG1, Host: Mouse, Monoclonal, Clone: KNH-30
Artikelnummer
BILCEL025
Verpackungseinheit
50 µg
Hersteller
BioLogo
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Clone: KNH-30.
Background: 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].
Positive Control: Diabetic lens cataract.
Immunogen: N-epsilon-(Carboxyethyl)-Lysine-BSA.
Purification Method: Protein G affinity purified antibody from ascites.
Concentration: 0.25 mg/ml.
References: 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.
Caution: 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.
Background: 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].
Positive Control: Diabetic lens cataract.
Immunogen: N-epsilon-(Carboxyethyl)-Lysine-BSA.
Purification Method: Protein G affinity purified antibody from ascites.
Concentration: 0.25 mg/ml.
References: 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.
Caution: 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.
| Artikelnummer | BILCEL025 |
|---|---|
| Hersteller | BioLogo |
| Hersteller Artikelnummer | CEL025 |
| Green Labware | Nein |
| Verpackungseinheit | 50 µg |
| Mengeneinheit | STK |
| Klonalität | Monoclonal |
| Methode | ELISA, Immunohistochemistry |
| Isotyp | IgG1 |
| Wirt | Mouse |
| Produktinformation (PDF) | Download |
| MSDS (PDF) |
|
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