Description
Key facts
Detection method:Colorimetric,
Sample types:Purified protein, Tissue Lysate, Plasma, Serum, Cell Lysate,
Assay type:Competitive,
Sensitivity:= 0.5 µg/mL,
Range:0.36 - 100 µg/mL,
Assay Platform:Microplate reader
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.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-Multi, Appropriate long-term storage conditions-Multi, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Advanced Glycation End-products (AGEs) are highly reactive compounds formed when reducing sugars non-enzymatically bind to proteins lipids or nucleic acids. They are often referred to as AGE products or AGE-BSA when in the form of bovine serum albumin (BSA). The molecular weight of AGE compounds can vary significantly due to the diversity of glycation products. AGEs express in various tissues but accumulate more in aging tissues and in certain pathological states. Detection of AGE products often utilizes AGE ELISA assays or fluorescence-based methods to measure AGE-BSA.
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.
AGE compounds play significant roles in the progression of diabetes and cardiovascular disease. In diabetes AGEs contribute to complications by modifying vascular structure and function where they link with proteins such as HbA1c in glycation. In cardiovascular disease AGE accumulation in vascular tissues enhances vascular stiffness and atherosclerotic lesion formation. The AGE-RAGE interaction perpetuates chronic inflammation further exacerbating these conditions.
