CircuLex CML-BSA /Nε-(Carboxymethyl)lysine-BSA

  • Applications
    • ELISA
  • Target CML/Nε-(Carboxymethyl)lysine
  • Code # CY-R2052
  • Size 200 µg
  • Price
    $222.79
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
  • Concentration:
    1.0 mg/mL
  • Description:

    CircuLex CML-BSA /Nε-(Carboxymethyl)lysine-BSA of 200 µg.

  • Formulation:
    The CML-BSA /Nε-(carboxymethyl) lysine-BSA is supplied frozen in a buffer containing 10mM PBS (pH 7.2).
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Product Type:
    Recombinant Protein
  • Research Area:
    Cell Biology
  • Short Description:

    CircuLex CML-BSA /Nε-(Carboxymethyl)lysine-BSA.

  • Size:
    200 µg
  • Storage Temperature:
    -20°C
  • Target:
    CML/Nε-(Carboxymethyl)lysine
Citations
  1. Anisuzzaman et al. Longistatin in tick saliva blocks advanced glycation end-product receptor activation. J Clin Invest. 124, 4429-44 (2014),
  2. W. Bao, D. Min, S. M. Twigg, N. A. Shackel, F. J. Warner, D. K. Yue, and S. V. McLennan; 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
References
  1. Ikeda K, et al.: Biochemistry 35: 8075 –8083, 1996
  2. Reddy S, et al.: Biochemistry 34: 10872 –10878, 1995
  3. Makino H, et al.: Kidney Int. 48: 517 –526, 1995 (
  4. Suzuki D, et al.: J Diabetes Complications 10: 314 –319, 1996
  5. Imai N, et al.: Nephron 76: 153 –160, 1997
  6. Murata T, et al.: Diabetologia 40: 764 –769, 1997
  7. Kume S, Takeya et al.: Am J Pathol. 147: 654 –667, 1995
  8. Sakata N, et al.: Atherosclerosis 141: 61 –75, 1998
  9. Sakata N, et al.: Atherosclerosis 142: 67 –77, 1999
  10. Kislinger T, et al.: J. Biol. Chem. 274: 31740 –31749, 1999