Human RAGE Biotinylated Antibody

Applications

Human RAGE Sandwich Immunoassay

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: RAGE/AGER

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).

Product Datasheets

Related Research Areas

• Adhesion Molecules in Angiogenesis
• APP Cleavage and Amyloid-beta Degradation
• Blood-brain Barrier Transporters
• Cell Structure and Signaling Molecules
• Cytokine and Growth Factor Receptors on VSMC
• Diabetes
• Diabetic Peripheral Neuropathy
• Glucose Homeostasis
• Immune Regulatory Molecules on Endothelial Cells
• Inflammatory Mediators
• Integrins and Associated Molecules
• Neurodegenerative Disease
• ROS and Stress Resistance