AGE (Advanced Glycation End) Assay Kit
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(1 Review)
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(8 Publications)
AGE (Advanced Glycation End Products) Assay Kit (ab238539) is designed for the rapid detection and quantitation of advanced glycation end product protein adducts.
View Alternative Names
AGEs, Advanced glycation end products
- cELISA
Supplier Data
Competitive ELISA - AGE (Advanced Glycation End) Assay Kit (AB238539)
Advanced Glycation End Product Formation Pathways.
CML = N-epsilon-(carboxymethyl)lysine.
GOLD = glyoxal-derived lysine dimer.
CEL = N-epsilon-(1-carboxyethyl)lysine.
MOLD = methylglyoxal-derived lysine dimer.
DOLD = 3-deoxyglucosone-derived lysine dimer.
3-DG = 3-deoxyglucosone.
- cELISA
Supplier Data
Competitive ELISA - AGE (Advanced Glycation End) Assay Kit (AB238539)
Example AGE-BSA Competitive ELISA Standard Curve.
Typical AGE Competitive ELISA results.
This data is for reference only and should not be used to interpret actual results.
Product details
AGE (Advanced Glycation End Products) Assay Kit (ab238539) is designed for the rapid detection and quantitation of advanced glycation end product protein adducts.
Advanced Glycation End Products (AGE) are formed during the Maillard reaction where reducing carbohydrates react with lysine side chains and N-terminal amino groups of various macromolecules, particularly proteins. The advanced glycation end products can adversely affect the fuction of these macromolecules. One of the most prevalent advanced glycation end products, N-epsilon-(Carboxymethyl) Lysine, has been implicated in oxidative stress and vascular damage. The quantity of AGE adduct in protein samples is determined by comparing its OD with that of a known AGE-BSA standard curve.
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Properties and storage information
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Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
AGE compounds affect cellular and tissue functions by altering structural proteins and increasing oxidative stress. While not a component of a specific complex AGEs catalyze cross-linking of proteins like collagen impacting tissue elasticity. The binding of AGEs to receptors such as RAGE (Receptor for Advanced Glycation End-products) triggers inflammatory pathways and oxidative stress. This interaction fuels the damaging effects of AGEs in biological systems which are assayed through AGE assays.
Pathways
AGE compounds influence several critical biological pathways particularly the NF-kB and MAPK pathways. These pathways mediate inflammation and cellular stress responses. The interaction with RAGE also affects signaling with related proteins like S100/calgranulins which further activate pro-inflammatory responses. The alteration of these pathways by AGE compounds highlights their significance in cellular dysfunction and age-related conditions.
Product protocols
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Publications (8)
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Journal of biochemical and molecular toxicology 38:e23515 PubMed37632267
2023
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Biomolecules 13: PubMed37371535
2023
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Diabetology & metabolic syndrome 14:99 PubMed35841066
2022
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BMC oral health 22:206 PubMed35614406
2022
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Molecular medicine reports 25: PubMed35211757
2022
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Biomedical reports 16:28 PubMed35251615
2022
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Journal of Alzheimer's disease : JAD 78:989-1010 PubMed33074237
2020
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Journal of periodontology 91:396-402 PubMed31389020
2019
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