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  • Anti CEL [NƒĂ-(carboxymethyl) lysine] Monoclonal Antibody

useful for potrcial role recerch of AGEs modification in nomal aging as well as age-enhanced desease processes

Anti CEL [NƒĂ-(carboxymethyl) lysine] Monoclonal Antibody


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Background

Reaction of protein amino groups with glucose leads, through the early products such as a Schiff base and Amadori rearrangement products, to the formation of advanced glycation end products (AGE). Recent immunological studies using anti-AGE antibody (6D12) demonstrated the presence of AGE-modified proteins in several human tissues: (1) human lens (nondiabetic and noncataractous), (2) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure, (3) diabetic retina, (4)@peripheral nerves of diabetic neuropathy, (5) atherosclerotic lesions of arterial walls, (6)β2-microglobulin forming amyloid fibrils in patients with hemodialysis-related amyloidosis, (7) senile plaques of patients with Alzheimer’s disease, (8) the peritoneum of CAPD patients, (9) skin elastin in actinic elastosis, and (10) ceriod/lipofuscin deposits. These results suggest a potential role of AGE-modification in normal aging as well as age-enhanced disease processes. This antibody named as 6D12 has been used to demonstrate AGE-modified proteins in these human tissues, indicating potential usefulness of this antibody for histochemical identification and biochemical quantification of AGE-modified proteins.

CEL is known to generate from protein modification by methylglyoxal . Mclellan et al. demonstrated that plasma methylglyoxal, which is believed to be generate from Embden-Meyerhof and polyol pathways, concentrations in insulin-dependent diabetic patients were about 7-times higher than those of normal individuals. For examples, CEL was identified in human lens proteins at a concentration similar to that of CML and its accumulation increased with age like CML, indicating that CEL may play an important marker for aging and age-dependent disease such as diabetic complications.


 AGEs Antibody Flyer [PDF]
 AGEs Antibody Flyer@(print file) [PDF]
Package Size 50μg  (200μL/vial)
Format
Buffer
Mouse monoclonal antibody 0.25 mg/mL
Block Ace as a stabilizer, containing 0.1% Proclin as a bacteriostat
Storage Store below  –20°C.
Once thawed, store at 4°C. Repeated freeze-thaw cycles should be avoided.
Clone No. KNH-30
Subclass IgG1
Purification method The splenic lymphocytes from BALB/c mouse, immunized with CEL-BSA were fused to myeloma P3U1 cells. The cell line (KNH-30) with positive reaction was grown in ascitic fluid of BALB/c mouse, from which the antibody was purified by Protein G affinity chromatography.
Working dilution for immunohistochemistry: 5-10μg/mL; for ELISA: 0.1-1.0μg/mL

<Reference>
References for CEL
A. Ahmed MU, Brinkmann E, Degenhardt TP, Thorpe SR, Baynes JW: Nε-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in humanlens proteins. Biochem J 324:565-570, 1997
B. Degenhardt TP, Thorpe SR, Baynes JW: Chemical modification of proteins by methylglyoxal. Cell Mol Biol 44:1139-1145, 1998
C. Mclellan AC, Thornalley PJ, Benn J, Sonksen PH: Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clinical Science 87: 21-29, 1994

*These references are the background of CEL , and are not this antibody examples

References for AGEs antibody
1. Horiuchi, S.et al.: Immunochemical approach to characterize advanced glycation end products of the Maillard reaction; Evidence for the presence of a common structure. J. Biol. Chem. 266: 7329, 1991.
2. Araki, N. et al.: Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging. J. Biol. Chem. 267: 10211, 1992.
3. Miyata, T. et al.: β2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. J. Clin. Invest. 92: 1243, 1993.
4. Yamada, K et al.: Immunohistochemical study of human advanced glycosylation end-products (AGE) in chronic renal failure. Clin. Nephrol. 42: 354, 1994.
5. Kume, S. et al.: Immunohistochemical and ultrasturactural detection of advanced glycation end products in atherosclerotic lesions of human aorta using a novel specific monoclonal antibody. Am. J. Pathol. 147 : 654, 1995.
6. Makino, H. et al.: Ultrastructure of nonenzymatically grycated mesangial matrix in diabetic nephropathy. Kidney International 48: 517, 1995.
7. Mori, T. et al.: Localization of advanced grycation end products of Maillard reaction in bovine tissues and their endocytosis by macrophage scavenger receptors. Exp. Molec. Pathol. 63:135, 1995
8. Miyata, T. et al.: Identification of pentosidine as a native structure for advanced glycation end products inβ2-Microglobulin forming amyloid fibrils in patients with dialysis-related amyloidsis. Proc. Natl. Acad. Sci. USA. 93: 2353, 1996
9. Kimura, T. et al.: Accumulation of advanced glycation end products of the Maillard reaction with age in human hippocampal neurons. Neurosci. Lett. 208: 53,1996.
10. Ikeda, K. et al.: Nε-(carboxymethyl) lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. Biochemistry 35: 8075,1996.

Product List

Product Name Cat# Quantity Price

Anti CEL, - (Mouse) Unlabeled DataSheet

KAL-KH025

50 UG ¥55,000
$734

Anti CEL, - (Mouse) Biotin DataSheet

KAL-KH025-01

50 UG ¥70,000
$934

Anti CEL, - (Mouse) Horseradish Peroxidase DataSheet

KAL-KH025-02

50 UG ¥70,000
$934

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