Welcome to Iris Biotech
For better service please confirm your country and language we detected.
Thank you very much for your interest in our products. All prices listed on our website are ex-works, Germany, and may attract customs duties when imported.
You may/will be contacted by the shipping company for additional documentation that may be required by the US Customs for clearance.
We offer you the convenience of buying though a local partner, Peptide Solutions LLC who can import the shipment as well as prepay the customs duties and brokerage on your behalf and provide the convenience of a domestic sale.Continue to Iris Biotech GmbHSend request to US distributor
Chemical name: Glyoxyl-derived lysine dimer acetic acid salt // Synonyms: 1,3-bis((S)-5-amino-5-carboxypentyl)-1H-imidazol-3-ium acetic acid salt
|CAS No.:||209267-39-0 net|
|Molecular weight:||327,40 g/mol|
Maillard Reaction Products (MRPs) are indicators for the heat treatment of food, as well as markers of nutritional quality. They also appear naturally in the human body as so-called Advanced Glycation End Products (AGEs). As such, they are indicators for body health and disease processes, including inflammation, diabetes, cancer and ageing. Consequently, AGEs gained broad attention in cosmetics, biochemistry, food, and pharmaceutical applications.
This material is supplied as a salt containing varying contents of the acid counterion. The net content of each batch is specified in the respective certificate of analysis.
Intact glycation end products containing carboxymethyl-lysine and glyoxal lysine dimer obtained from synthetic collagen model peptide; H. Yamada, T. Sasaki, S. Niwa, T. Oishi, M. Murata, T. Kawakami and S. Aimoto; Bioorg Med Chem Lett 2004; 14: 5677-80. https://doi.org/10.1016/j.bmcl.2004.08.044
Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes; P. Chellan and R. H. Nagaraj; Archives of biochemistry and biophysics 1999; 368: 98-104. https://doi.org/10.1006/abbi.1999.1291
Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteins; E. B. Frye, T. P. Degenhardt, S. R. Thorpe and J. W. Baynes; J Biol Chem 1998; 273: 18714-9. https://doi.org/10.1074/jbc.273.30.18714
Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: evidence for increased oxidative stress in uremia; H. Odani, T. Shinzato, J. Usami, Y. Matsumoto, E. Brinkmann Frye, J. W. Baynes and K. Maeda; FEBS Lett 1998; 427: 381-5. https://doi.org/10.1016/s0014-5793(98)00416-5
Characterization of an Imidazolium Salt Formed from Glyoxal and N.alpha.-Hippuryllysine: A Model for Maillard Reaction Crosslinks in Proteins; K. J. Wells-Knecht, E. Brinkmann and J. W. Baynes; The Journal of Organic Chemistry 1995; 60: 6246-6247. https://doi.org/10.1021/jo00125a001
Do you need larger quantities for your development or production?
Please send me more information about