CircuLex CML/Nε-Carboxymethyl)lysine ELISA Kit

  • Applications
    • ELISA
  • Code # CY-8066
  • Size 96 Assays
  • Price
    $593.74
Specifications

Background

Reducing sugars react with protein amino groups to form a diverse group of protein-bound moieties with fluorescent and cross-linking properties. These compounds, called advanced glycosylation end products (AGEs), have been implicated in the structural and functional alterations of proteins that occur during aging and long-term diabetes. Although several AGE structures have been reported (1, 2), it was demonstrated that Nε-(carboxymethyl) lysine (CML) is a major antigenic AGE structure. CML concentration is also increased in patients who have diabetes with complications, including nephropathy (3–5), retinopathy (6), and atherosclerosis (7–9). CML is also recognized by receptor for AGE (RAGE), and CML-RAGE interaction activates cell signaling pathways such as NF-B and enhances the expression of vascular cell adhesion molecule-1 in human umbilical vein endothelial cells (10).
  • Application:
    ELISA
  • Components:
    • CML-BSA coated Microplate
    • Wash Buffer
    • Sample Dilution Buffer
    • Standard Dilution Buffer
    • CML-HSA Standard
    • Primary Antibody
    • HRP conjugated Detection Antibody
    • Substrate Reagent
    • Stop Solution
  • Description:

    The CycLex Research Product CircuLex CML/Nε-(carboxymethyl) lysine ELISA Kit is used for the quantitative measurement of CML-adducts in mammalian serum, plasma, tissue extract and other biological media except rodent specimen. It can be used for 96 Assays.

  • Product Type:
    ELISA Kit
  • Research Area:
    Metabolism
  • Short Description:

    CircuLex CML/Nɛ-Carboxymethyl)lysine ELISA Kit.

  • Size:
    96 Assays
Citations
  1. Aoki C et al. Advanced glycation end products suppress lysyl oxidase and induce bone collagen degradation in a rat model of renal osteodystrophy. Lab Invest. 93, 1170-83 (2013),
  2. Bao W et al. Monocyte CD147 is induced by advanced glycation end products and high glucose concentration: possible role in diabetic complications. Am J Physiol Cell Physiol. 299, C1212-C1219 (2010),
  3. Boschetto P et al. Plasma sRAGE and N-(carboxymethyl) lysine in patients with CHF and/or COPD. Eur J Clin Invest. 43, 562-9 (2013),
  4. Coughlan MT et al. Advanced Glycation Urinary Protein-Bound Biomarkers and Severity of Diabetic Nephropathy in Man. Am J Nephrol. 34, 347-355 (2011),
  5. Fujii EY, Nakayama M. The measurements of RAGE, VEGF, and AGEs in the plasma and follicular fluid of reproductive women: the influence of aging. Fertility and Sterility. 94, 694-700 (2010),
  6. Han D et al. Induction of receptor for advanced glycation end products by insufficient leptin action triggers pancreatic β-cell failure in type 2 diabetes. Genes Cells. 18, 302-14 (2013),
  7. Karimi J et al. Relationship between advanced glycation end products and increased lipid peroxidation in semen of diabetic men. Diabetes Res Clin Pract. 91, 61-6 (2011),
  8. Lance A et al. Apolipoprotein E4 Exaggerates Diabetic Dyslipidemia and Atherosclerosis in Mice Lacking the LDL Receptor. Diabetes. 60, 2285-2294 (2011),
  9. Machado-Lima A et al. Advanced glycated albumin isolated from poorly controlled type 1 diabetes mellitus patients alters macrophage gene expression impairing ABCA-1-mediated reverse cholesterol transport. Diabetes Metab Res Rev. 29, 66-76 (2013),
  10. Machado-Lima A et al. In type 2 diabetes mellitus glycated albumin alters macrophage gene expression impairing ABCA1-mediated cholesterol efflux. J Cell Physiol. 230, 1250-7 (2014),
  11. Malarde L et al. Endurance training and insulin therapy need to be associated to fully exert their respective beneficial effects on oxidant stress and glycemic regulation in diabetic rats. Free Radic Res. 48, 412-9 (2014),
  12. Meloche J et al. RAGE-dependent activation of the oncoprotein Pim1 plays a critical role in systemic vascular remodeling processes. Arterioscler Thromb Vasc Biol. 31, 2114-24 (2011),
  13. Moriyama T et al. Involvement of advanced glycation end-products, pentosidine and N-(carboxymethyl)lysine, in doxorubicin-induced cardiomyopathy in rats. Toxicology. 268, 89-97 (2010),
  14. Munesue S et al. Low-molecular weight fractions of Japanese soy sauce act as a RAGE antagonist via inhibition of RAGE trafficking to lipid rafts. Food Funct. 4, 1835-42 (2013),
  15. Nemoto S et al. Aminoguanidine normalizes ET-1-induced aortic contraction in type 2 diabetic Otsuka Long-Evans Tokushima Fatty (OLETF) rats by suppressing Jab1-mediated increase in ET(A)-receptor expression.; Peptides. 33, 109-19 (2012),
  16. Pettersson C et al. LDL-associated apolipoprotein J and lysozyme are associated with atherogenic properties of LDL found in type 2 diabetes and the metabolic syndrome. J Intern Med. 269, 306-21 (2011),
  17. Tahara N et al. Serum levels of advanced glycation end products (AGEs) are independent correlates of insulin resistance in nondiabetic subjects. Cardiovasc Ther. 30, 42-8 (2012),
  18. Xianwen Yi et al. α-Lipoic acid protects diabetic apolipoprotein E-deficient mice from nephropathy. Journal of Diabetes and its Complications. 25, 193-201 (2011),
  19. Zuwa?a-Jagie??o J et al. Advanced oxidation protein products and inflammatory markers in liver cirrhosis: a comparison between alcohol-related and HCV-related cirrhosis. Acta Biochim Pol. 58, 59-65 (2011)
References
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  3. Makino H, Shikata K, Hironaka K, Kushiro M, Yamasaki Y, Sugimoto H, Ota Z, Araki N, Horiuchi S: Kidney Int 48: 517 –526,1995
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  5. Imai N, Nishi S, Suzuki Y, Karasawa R, Ueno M, Shimada H, Kawashima S, Nakamaru T, Miyakawa Y, Araki N, Horiuchi S, Gejyo F, Arakawa M: Nephron 76: 153 –160,1997
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  10. Kislinger T, Fu C, Huber B, Qu W, Taguichi A, Du Yan S, Hofmann M, Yan SF, Pischetsrieder M, Stern D, Schmidt AM: J Biol Chem 274: 31740 –31749,1999