Advanced Glycation Endproducts
3 new Competitive ELISA kits for advanced glycation endproducts:
- HIT501, Nitrotyrosine Competitive ELISA
When the formation of reactive oxygen species (ROS) exceeds the removal by scavenger systems, e.g. by the action of superoxide dismutase (SOD), catalase and peroxidases, this can lead to a multitude of pathological conditions:
- Diabetes
- Parkinson’s disease
- Alzheimer’s disease
- Rheumatoid arthritis
- Inflammatory bowel diseases
- Chronic inflammation
- Sepsis
Coming Soon:
- HIT502, CML Competitive ELISA
- HIT503, MGO Competitive ELISA
Glycation, or non-enzymatic glycosylation, is the non-enzymatic reaction of glucose and other reducing sugars with free amino groups of proteins, lipids and nucleic acids. The amino groups of the side chains of arginine and lysine are the primary targets for this type of modification. Over time, the initial glycation products may undergo intramolecular rearrangements and oxidation reactions (glycoxidation) and ultimately transfrom in stable, so-called advanced glycation end products (AGEs). Several compounds, e.g. NƐ-carboxymethyl-lysine (CML), pentosidine, or methylglyoxal derivates (MGO), serve as examples of well-characterized and widely studies AGEs.
AGEs have the potential to interact with a specific receptor (RAGE), a member of the immunoglobulin superfamily, initiating signal pathways that amplify infammation and oxidative stress, and thereby leading to cellular injury and death. High levels of circulating AGEs are associated with cardiovascular disease, diabetes, chronic kidney disease, and increased mortality.
For more information regarding MGO, please click here.