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useful for research of potencial role of AGEs modification in nomal ging as well as age-enhanced disease processes

Anti AGEs [Advanced Glycation End Products] 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)eriod/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.


 AGEs Antibody Flyer [PDF]
 AGEs Antibody Flyer@(print file) [PDF]

ySpecificityz
The initial study (Ref. 1) revealed that 6D12 does not recognize early products (Schiff base and Amadori products), but shows a positive reaction to AGE-samples obtained either from proteins, lysine derivatives or monoamino-carboxylic acids, indicating the immunospecificity to a common structure among AGE-structures. The subsequent study (Ref. 10) revealed of 6D12 is an Nε- carboxymethyllysine(CML)-protein adduct.


‚OImmunohistochemical staining of renal proximal tubules and glomeruli in patients with diabetic nephropathy, using anti-AGE antibody 6D12
Yamada, K. et al,.Clinical nephrology, Vol.42, 354-361, 1994

Immunohistochemical staining of th eary stage of@human athrosclerotic lesions of the aorta with anti-AGE antibody 6D12.
Kume, S. et al,American Journal of Pathology, Vol.147, 654-667, 1995
Package Size 10µg  (40µL/vial)
Format Mouse monoclonal antibody @0.25 mg/mL
Buffer Block Ace as a stabilizer, containing 0.1%Proclin as bacteriostat
Storage Store below  –20°C
Once thawed, store at –4°C. Repeated freeze-thaw cycles should be avoided.
Clone No. 6D12
Subclass IgG1
Purification Method The splenic lymphocytes from BALB/c mouse, immunized with AGE-BSA were fused to myeloma P3U1 cells. The hybrid cells were screened, and the cell line (6D12) with positive reaction to AGE-human serum albumin but negative to BSA was selected through successive subclonings and grown in ascitic fluid of BALB/c mouse, from which the anti-AGE antibody was purified by Protein G affinity chromatography. (Reference No.1)
Working dilution for immunohistochemistry: 2µg /mL; for ELISA: 0.1-0.5µg /mL; for WB : 0.25-5µg /mL

 

<Reference>
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.

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