MCP-1 Human Recombinant Protein

MCP-1, or Monocyte chemoattractant protein 1, of the intercrine beta (chemokine CC) family, is a chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. It augments monocyte anti-tumor activity and has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. It may be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. MCP-1 exists as a monomer or homodimer; in equilibrium. It binds to CCR2 and CCR4 and is tethered on endothelial cells by glycosaminoglycan (GAG) side chains of proteoglycans. Processing at the N-terminus can regulate receptor and target cell selectivity. Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant. Recombinant Human MCP-1 produced in E. coli is a non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8607 Daltons.