Description
Product details:
ab219802 enables the highly sensitive detection of glycated proteins (advanced glycation endproducts, AGEs) using a simple polyacrylamide gel electrophoresis (PAGE)-based method. This kit is compatible with a range of biological samples, including lysates, plasma, sera or tissue homogenates.
Glucose and other metabolites of glycolysis react directly with important cellular components such as DNA, lipids and protein through a process known as glycation. During glycation, reducing sugar molecules react with the amino groups of amino acids such as those found on lysine, arginine and protein N-termini, ultimately leading to the formation of complex and stable AGEs.
This kit uses Fluorescein-phenylboronate gel electrophoresis (Flu-PAGE) to detect early glycation adducts on proteins by exploiting the reversible covalent interaction between boronic acid and
-diols that are present in fructosamine-protein adducts in glycated proteins (
Pereira Morais et al., 2013
). This interaction is further strengthened by the additional charge interaction between boronate and the fructosylysine amino group (
Pereira Morais et al., 2010
). As the anomeric cis diols produced by this interaction are absent in
-glycosylation, this method enables the specific identification of glycated proteins over glycosylated and unmodified proteins as (
Pereira Morais et al., 2013; Kassaar et al., 2017
). This highly sensitive method detects the earliest stages of glycation, before AGEs are developed, and thus is an ideal tool for identifying reducing sugar modified proteins in complex biological samples such as plasma and brain homogenates.
Properties and Storage Information:
Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Glycated protein forms when proteins covalently bond with sugar molecules a process known as glycation. This target frequently termed as glycosylated protein can also vary significantly in mass depending on the protein's specific type and number of attached sugar residues. Glycated proteins express widely in tissues and body fluids such as blood where they play essential roles in biological systems. Biomedical research commonly utilizes it for understanding mechanisms regulating protein function and interactions.
Biological function summary
Glycated proteins impact physiological and biochemical pathways by altering normal protein function. They often interact with different cellular signals and can form part of larger complexes influencing stability and recognition of proteins within the cell. The alteration derived from glycation may affect a protein's structural conformation leading to misfolding and subsequent loss or gain of function; this can impact cellular communication and metabolism.
Pathways
Glycated proteins actively participate in metabolic and signalling pathways such as carbohydrate metabolism and the insulin signalling pathway. These pathways involve various other proteins including glucose transporters and enzymes regulating metabolic processes. Glycation might modify these pathways interacting with proteins that play roles in glucose regulation and energy balance thereby impacting cellular homeostasis.
Glycated proteins closely associate with diabetes and cardiovascular disease. In diabetes prolonged blood glucose elevation leads to increased glycation affecting proteins like hemoglobin forming hemoglobin A1c a marker for glucose management. Cardiovascular disorders relate to altered glycated proteins since excessive glycation can induce endothelial dysfunction disrupting normal vascular functions and contributing to disease pathology. Glycated albumin and other serum proteins often serve as markers illustrating the clinical significance of protein glycation within these disease contexts.
