AGE, Advanced Glycation End ProductsCatalogue number: AGE101-0.2
IHC not established
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 colour 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%.
Immunogen: Advanced Glycation End Products /BSA/HSA
Serum containing 0.1% sodium azide
Purification Method: Serum containing 0.1% sodium azide
Secondary Reagents: We recommend the use of BIOLOGO's Universal Staining System DAB (Art. No. DA005) or AEC (Art. No. AE005).
Species Reactivity: Human
ELISA, IHC not established
Incubation Time: 60 min at RT or 18 hr at 2-8°C
Working Concentration: (liquid conc.) 1:5000 - 1:25000 ELISA
Positive Control: human lens, arteriosclerotic plaques
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. ** The preservative sodium azide is known to be poisonous and potentially hazardous to health. It should be handled only by trained staff. Despite of the product's low azide concentration it must be handled with care. Dispose according to regional rules!
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. Akari 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.
AGE, Advanced Glycation End Products