esRAGE Human ELISA Kit

Applications: Metabolics/Obesity/Diabetes
Categories: Assay Kits

The kit specifically detects the endogenous secreted form of RAGE (i.e. esRAGE) in human plasma and serum samples. The esRAGE protein has been implicated in physiological changes associated with diabetes, Alzheimer''s, and vascular disease. The microplate is pre-coated with primary anti-esRAGE antibody. The secondary esRAGE antibody conjugated to HRP is added for detection. After incubation, 3,3'',5,5''-tetramethylbenzidine (TMB) and hydrogen peroxide are added as a colorimetric substrate for color development. Color is measured at 450 nm.

Reactivity: Human
Sample Type: Serum, plasma, and tissue culture medium
Range: 0.05 - 3.2 ng/ml
Limit of Detection: 0.025 ng/ml


  1. Brownlee, M, Cerami, A, and Vlassara, H. Advanced glycosylation end products in tissue and thebiochemical basis of diabetic complications. N. Engl. J. Med. 318:1315-1321 (1988).
  2. Harding, J.J. Nonenzymatic covalent posttranslational modification of proteins in vivo. Adv. ProteinChem. 37:248-334 (1985).
  3. Sakurai, S, Yonekura, H, Yamamoto, Y, Watanabe, T, Tanaka, N, Li, H, Azadur Rahman, A.K.M,Myint, K.M, Kim, C.H, and Yamamoto, H. The AGE-RAGE system and diabetic nephropathy. J.Am Soc Nephrol 14:S259-S263 (2003)
  4. Wautier, J.L, Wautier, M.P, Schmidt, A.M, Anderson, G.M, Hori, O, Zoukourian, C, Capron, LO,Chappey, O, Yan, S.D, Brett, J, et al. Advanced glycation end products (AGEs) on the surface ofdiabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in thevasculature: a link between surface-associated AGEs and diabetic complications. Proc. Natl. Acad.Sci. USA Aug 2; 91(16):7742-7746 (1994).
  5. Münch, G, Kuhla, B, Lüth, H.J, Arendt, T, and Robinson, S.R. Anti-AGEing defences againstAlzheimer’s disease. Biochem. Soc. Trans. 31:1397-1399 (2003).
  6. Schmidt, A.M, Vianna, M, Gerlach, M, Brett, J, Ryan, J, Kao, J, Esposito, C, Hegarty, H, Hurley, W,Clause, M, Wang, F, Pan, Y.C.E, Tsang, T.C, and Stern, D. Isolation and characterization of twobinding proteins for advanced glycosylation end products from bovine lung which are present onthe endothelial surface. J. Biol. Chem. 267:14987-14997 (1992).
  7. Neeper, M, Schmidt, A.M, Brett, J, Yan, S.D, Wang, F, Pan, Y.C.E, Elliston, K, Stern, D, and Shaw,A. Cloning and expression of a cell surface receptor for advanced glycosylation end products ofproteins. J. Biol. Chem. 267:14998-15004 (1992).
  8. Brett, J, Schmidt, A.M, Yan, S.D, Zou, Y.S, Weidman, E, Pinsky, D, Nowygrod, R, Neeper, M,Przysiecki, C, Shaw, A, Migheli, A, and Stern, D. Survey of the distribution of newly characterizedreceptor for advanced glycation end products in tissues. Am. J. Pathol. 143:1699-1712 (1993).
  9. Yan, S.D, Schmidt, A.M, Anderson, G.M, Zhang, J, Brett, J, Zou, Y.S, Pinsky, D, and Stern, D.Enhanced cellular oxidant stress by the interaction of advanced glycation end products with theirreceptors/binding proteins. J. Biol. Chem. 269:9889-9897 (1994).
  10. Lander, H.M, Tauras, J.M, Ogiste, J.S, Hori, O. Moss, R.A, and Schmidt, A.M. Activation of thereceptor for advanced glycation end products triggers a p21ras-dependent mitogen-activatedprotein kinase pathway regulated by oxidant stress. J. Biol. Chem. 272:17810-17814 (1997).
  11. Schmidt, A.M, and Stern, D.M. RAGE: a new target for the prevention and treatment of thevascular and inflammatory complications of diabetes. Trends Endocrinol. Metab. 11:368-375(2000).
  12. Tanaka, N, Yonekura, H, Yamagishi, S, Fujimori, H, Yamamoto, Y, and Yamamoto, H. The receptorfor advanced glycation end products is induced by the glycation products themselves and tumornecrosis factor-a through nuclear factor kB, and by 17b-estradiol through Sp-1 in human vascularendothelial cells. J. Biol. Chem. 275:25781-25790 (2000).
  13. Yonekura, H, Yamamoto, Y, Sakurai, S, Petrova, R.G, Abedin, J, Li, H, Yasui, K, Takeuchi, M,Makita, Z, Takasawa, S, Okamoto, H, Watanabe, T, and Yamamoto, H. Novel splice variant of thereceptor for advanced glycation end-products expressed in human vascular endothelial cells andpericytes, and their putative roles in diabetes-induced vascular injury. Biochem. J. 370:1097-1109(2003).