Anti-RAGE (Human) mAb

WB - 0.5-1 ug/mL

RAGE is a multi-ligand member of the immunoglobulin superfamily of cell surface molecules that is expressed in a variety of cell lines, including end othelial cells, smooth muscle cells, mononuclear phagocytes, pericytes, neurons, cardiac myocytes, mesangial cells and hepatocytes (1, 2). RAGE interacts with different structures to transmit a signal into the cell and recognizes three-dimensional structures rather than specific amino acid sequences. Therefore, RAGE seems to fulfill the requirements of a pattern-recognition receptor. As a member of the immunoglobulin superfamily, it interacts with a diverse class of ligands, including AGEs (3, 4), HMGB1 (also known as Amphoterin) (5), amyloid β-peptide (6), amyloid A (7), leukocyte adhesion receptors (8), prions (9), Escherichia coli curli operons (10), β-sheet fibrils (11) and several members of the S100 protein superfamily including S100/calgranulins (12). Thus RAGE may have potential involvement in several pathological processes including inflammation, diabetes, Alzheimer?s disease (AD), systemic amyloidosis, and tumor growth (13). It has been reported that soluble RAGE (sRAGE) isoforms that could act as decoy receptors may be cleaved proteolytically from the native RAGE expressed on the cell surface (14), as well as endogenous secretory RAGE (esRAGE) derived from a splice variant, carrying all of the extracellular domains. This proteolytic generation of sRAGE was initially descr ibed as occurring in mice (15). These diverse types of sRAGE in human plasma could exert significant protective effects against RAGE-mediated toxicity.

1.0 ug/uL

20 mM phosphate buffer (pH 7.5), 300 mM NaCl, 50 % glycerol.

Extracellular domain of Recombinant human RAGE

46-54 kDa

1 year

The antibody is produced by immunizing mice with a recombinant extacellular domain of human RAGE. IgG is purified by protein A-Sepharose chromatography.

RAGE