AGE, Advanced Glycation End ProductsCatalog number: AGE102-1.0
This antibody is suitable for the detection of different AGE products in tissues, tissue extracts and body fluids. 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. These results suggested the potential role of AGE in normal aging and age-enhanced disease processes. Advanced Glycation End Products (AGE), cross-reactivity BSA and HSA <1%.
Serum from rabbits immunized with Advanced Glycation End Products /BSA/HSA
Immunogen: Advanced Glycation End Products /BSA/HSA
Protein A affinity purified IgG in PBS 0.05 M; pH 7.15; 0.85% NaCl; 0.05% sodium azide**
Purification Method: Protein A affinity purified IgG in PBS pH 7.15 containg 0.05% sodium azide**
Secondary Reagents: We recommend the use of BIOLOGO's Universal Staining System DAB (Art. No. DA005) or AEC (Art. No. AE005).
Concentration: Approximately 1mg/ml
Species Reactivity: Human
ELISA, IHC not established
Incubation Time: 60 min at RT or 18 hr at 2-8°C
Working Concentration: (liquid conc.) ELISA app. 1 µg/ml, (IHC 5-10 µg/ml)
Positive Control: human lens, arteriosclerotic plaques
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. It may contain hazardous ingredients. Please refer to the Safety Data Sheets (SDS) for additional information and proper handling procedures. Dispose product remainders according to local regulations.This datasheet is as accurate as reasonably achievable, but Exalpha Biologicals accepts no liability for any inaccuracies or omissions in this information.
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. Araki N., Ueno N., Chakrabarti B., Morino Y., and Horiuchi S. (1992) Immunochemical evidence of the presence of advanced glycation end products in human lens proteins and its positive correlation with aging. J. Biol. Chem. 267; 10211-10214. 3. Miyata T., Odo O., Inagi R., Iida Y., Araki N., Yamada N., Horiuchi S., Taniguchi N., Maeda, et al. (1993) ß2-Microglobulin modified with advanced glycation end products is a major component of haemodialysis-associated amyloidosis. J. Clin. Invest. 92; 1243-1252. 4. Kume S., Takeya M., Mori T., Araki N., Suzuki H., Horiuchi S., Kodama T., Miyauchi Y., and Takahashi K. (1995) Immunohistochemical and ultrastructural detection of advanced glycation end products in atherosclerotic lesions of human aorta using a novel specific monoclonal antibody. Am J. Pathol. 147; 654-667. 5. Kimura T., Takamatsu J., Ikeda K., Kondo A., Miyakawa T., and Horiuchi S. (1996) Accumulation of advanced glycation end products of the Maillard reactionwith age in human hippocampal neurons. Neurosci. Lett. 208; 53-56.
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