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(anti-Human and others as indicated)

RDI Divison of researchd Industries Intl  offers a wide line of  antibodies. Since no one antibody works best for all applications (neutralization, blotting, histochemistry, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.

cat#RDI-ADVGLYabm    Advanced Glycosylation  6D12 mIgG    5ug $1295.00  

note: we regret the producer has more than doubled their price on this product effective July 2001 so we now offer the 5ug size only

-see other AGE related abs in pdf format   age-mabs.pdf

special order from Japan, takes approx 2 weeks for delivery  after order.

AGE Formation in vivo:

- Diabetic complications

- Atherosclerosis

- Alzheimer's disease

AGE Formation in vitro:

- Melanoidin Formation in Food

- Food Processing and Storage

Anti-AGE Antibody Technical Information

Reaction of amino groups in protein with glucose leads to the formation of advanced glycation end products (AGE) through the early products such as Schiff base and Amadori rearrangement products.

Recent immunological studies using anti-AGE antibody (6D12) demonstrated the presence of AGE-modified proteins in several human tissues:

(I) human lens (non-diabetic and non-cataractous),

(ii) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure,

(iii) diabetic retina,

(iv) peripheral nerves of diabetic neuropathy,

(v) atherosclerotic lesions of arterial walls,

(vi) b2-microglobulin forming anyloid fibrils in patients with hemodialysis-related amyloidosis,

(vii) senile plaques of patients with Alzheimer disease,

(viii) peritoneum of CAPD patients,

(ix) skin elastin in actinic elastosis, and

  (x) ceroid/lipofusion 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 the antibody for histochemical identification and biochemical quantification of AGE-modified proteins. 6D12 does not recognize the early products, Schiff base and Amadori products. It, however, shows positive reaction to AGE-samples obtained either from proteins, lysine derivatives, or monoamino-carboxylic acids. This result indicates the immunospecificity of 6D12 to a common structure among AGE-structures. The epitope of 6D12 is an N3-carboxymethyllysine (CML)-protein adduct. This antibody also recognizes carboxyethyllysine. New antibodies, specific for advanced glycation end products (AGE products), will be added shortly.

[Package and properties]

Package: 5ug    (0.25 mg/ml in PBS).

Clone Number: mouse monoclonal antibody 6D12.

Class: IgG1, mouse monoclonal antibody

Working concentration for immunohistochemistry (2 ug/ml) and

ELISA (0.1-0.5 ug/ml)


The initial study (Horiuchi, et al., 1991) 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 mono amino-carboxylic acids, indicating the immunospecificity to a common structure among AGE-structures. The subsequent study (Ikeda, et al., 1996) revealed the epitope of 6D12 is an N e-carboxymethyllysine (CML)-protein adduct.

.References .

1. Horiuchi, 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.: � 2-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 ofpentosidine as a native structure for advanced glycation end products in � 2-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.: Ne-(carboxymethyl) lysine protein adduct is a major immunological epitope in proteins modified withadvanced glycation end products of the Maillard reaction. Biochemistry 35: 8075,1996.

11. Horiuchi, S. et al.: AGE modified proteins and their potential relevance to atherosclerosis. Trends Cardiovasc. Med. 6: 163, 1996.

12. Hammes, H-P et al.:Modification of vitronectin by advanced glycation alters functional properties in vitro and in the diabetic retina. Lab. Invest. 75: 325, 1996.

13. Kimura, T. et al.: Identification of advanced grycation end products of the Maillard reaction in Pick�s disease. Neurosci. Lett. 219: 95, 1996.

14. Nakayama, M. et al.: immunohistochemical detection of advanced grycosylation end-products in the peritoneum and its possible pathophysiological role in CAPD. Kidney Intentional 51: 182, 1997.

15.Mizutani, K. et al.: Photo-enhanced modification of human skin elastin in actinic elastosis by Ne-  carboxymethyl)lysine,one of the glycoxidation products of the Maillard reaction. J. Invest. Dermatol. 108: 797, 1997.

16. Murata, T. et al.: The relationship between expression of advanced glycation end products and vascular endothelial growth factor in human diabetic retinas. Diabetologia 40: 764, 1997.

17. Sugimoto, K. et al.: Localization in human diabetic peripheral nerve of Ne-carboxymethyllysine-protein adducts, one of advanced glycation endproducts. Diabetologia 40: 1380, 1997.

18. Shimokawa, I. Et al.: Advanced glycosylation end-products in adrenal lipofuscin. J. Gerontol. 51A: B49, 1998.

19. Yoshida, S. et al.: Immunohistochemical study of human advanced glycation end-products and growth factors in cardiac tissues of patients on maintenance dialysis and with kidney transplantation. Clin. Nephrol.49:273, 1998.

20. Matsuse, S. et al.: immunohistochemical localisation of advanced glycation end products in pulmonary fibrosis. J. Clin. Pathol, 51: 515 ,1998


cat #RDI-ADVGLY-HRP     $1062.00/10ug     $2000.00/20ug

Presentation: affinity purified frozen liquid (F(ab')2   Anti-AGE, HRP-conjugated

Clone: 6D12

Isotype: mouse IgG1

Applications: Immunohistochemistry at 2 �g/ml;

                       ELISA at 0.1-0.5 �g/ml

Specificity: Broad spectrum advanced AGE products of the Maillard reaction, such as AGE-serum protein (BSA, HAS, Hb, Collagen);AGE-poly-Lys; AGE-Lys-derivatives; AGE-monoaminocarboxylic acids. Negative reaction for early stage products of Maillard reaction (Schiff base adducts and Amadori products), unmodified products, unmodified poly-lys and derivatives, unmodified monoamino carboxylic acids and other products (FFI, Pyrrole and Pentosidine).

For Research Use Only

Advanced Glycation Endproduct (AGE)-BSA

RDI-ADVGLY-AG    $440.00/10mg vial

AMOUNT: 10 mg (10 mg/ml in PBS)

FORM: Liquid. Supplied in 1X PBS (10 mg/ml). 0.22 �m filter sterilized

STORAGE: Store at 4 o C for up to 1 week or -70 o C for long-term storage.

PURITY: >98%

DESCRIPTION: The AGE modified BSA was produced by reacting BSA with glycolaldehyde under sterile conditions followed by extensive dialysis and purification steps. Fluorescence of AGEs was confirmed by fluorescence spectrophotometry with Ex./Em. = 370/440 nm. Glycated BSA shows a 7000% increase in fluorescence in compared to control BSA.

NOTE: During extended storage, AGE-BSA may precipitate. In this case, sonication will be helpful to dissolve the precipitates.

REFERENCE: Farboud, B., et al. (1999) Molecular Vision 5:11.

For In Vitro research Use Only

RDI Div of researchd Industries Intl

(Research Diagnostics Inc)

San Jose, 95123 CA Snell ave 658


or 408-780-0908


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