• Purity

  >90%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. rhRAGE/Fc Chimera immobilized at 5 µg/mL (100 µL/well) on a goat anti-human IgG Fc antibody-coated plate (0.5 µg/well) can bind biotinylated advanced glycation endproducts of bovine serum albumin (AGE-BSA, Catalog # BT4127) with a linear range of 0.02-1 µg/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Human RAGE (Gln24 - Ala344) Accession # Q15109	IEGRMD	Human IgG1 (Pro100 - Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  No results obtained: Gln24 predicted

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  61 kDa (monomer)

• SDS-PAGE

  80-90 kDa, reducing conditions

Background: RAGE

Advanced glycation endproducts (AGE) are adducts formed by the non-enzymatic glycation or oxidation of macromolecules (1). AGE forms during aging and its formation is accelerated under pathophysiologic states such as diabetes, Alzheimer’s disease, renal failure and immune/inflammatory disorders. Receptor for Advanced Glycation Endoproducts (RAGE), named for its ability to bind AGE, is a multi-ligand receptor belonging the immunoglobulin (Ig) superfamily. Besides AGE, RAGE binds amyloid beta -peptide, S100/calgranulin family proteins, high mobility group B1 (HMGB1, also know as amphoterin) and leukocyte integrins (1, 2).

The human RAGE gene encodes a 404 amino acid residues (aa) type I transmembrane glycoprotein with a 22 aa signal peptide, a 320 aa extracellular domain containing an Ig-like V-type domain and two Ig-like Ce-type domains, a 21 aa transmembrane domain and a 41 aa cytoplasmic domain (3). The V-type domain and the cytoplasmic domain are important for ligand binding and for intracellular signaling, respectively. Two alternative splice variants, lacking the V-type domain or the cytoplasmic tail, are known (1, 4). RAGE is highly expressed in the embryonic central nervous system (5). In adult tissues, RAGE is expressed at low levels in multiple tissues including endothelial and smooth muscle cells, mononuclear phagocytes, pericytes, microglia, neurons, cardiac myocytes and hepatocytes (6). The expression of RAGE is upregulated upon ligand interaction. Depending on the cellular context and interacting ligand, RAGE activation can trigger differential signaling pathways that affect divergent pathways of gene expression (1, 7). RAGE activation modulates varied essential cellular responses (including inflammation, immunity, proliferation, cellular adhesion and migration) that contribute to cellular dysfunction associated with chronic diseases such as diabetes, cancer, amyloidoses and immune or inflammatory disorders (1).

• References:

1. Schmidt, A. et al. (2001) J. Clin. Invest. 108:949.

2. Chavakis, T. et al. (2003) J. Exp. Med. 198:507.

3. Neeper, M. et al. (1992) J. Biol. Chem. 267:14998.

4. Yonekura, H. et al. (2003) Biochem. J. 370:1097.

5. Hori, O. et al. (1995) J. Biol. Chem. 270:25752.

6. Brett, J. et al. (1993) Am. J. Pathol. 143:1699.

7. Valencia, J.V. et al. (2004) Diabetes 53:743.

• Long Name:

  Receptor for Advanced Glycation End Products

• Entrez Gene IDs:

  177 (Human); 11596 (Mouse); 81722 (Rat)

• Alternate Names:

  AGER; EC 2.7.11.22; MOK protein kinase; MOKMAPK/MAK/MRK overlapping kinase; RAGE; RAGE-1; RAGE1renal cell carcinoma antigen (MOK protein kinase); Renal tumor antigen 1; renal tumor antigen