Anti-A2M / Alpha-2-Macroglobulin, clone A2M/4847

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Alpha-2-Macroglobulin (Alpha-2M) is a homotetrameric serum protein consisting of four identical subunits that form dimers through disulfide bonds. Initially, Alpha-2M was characterized as a pan-proteinase inhibitor that was able to bait proteinases into cleaving specific peptide sequences on Alpha-2M. This interaction induces a conformational change in Alpha-2M, thus enabling it to trap the proteinase and further inhibit its activity. Subsequently, Alpha-2M has been shown to function as a carrier protein and regulator of cytokines during inflammation. Circulating transforming growth factor beta (TGFbeta) in serum is primarily bound to Alpha-2M, which renders TGFbeta inactive. Alpha-2M also binds to IL-6 and, thereby, increases the concentration of IL-6 near lymphocytes, hepatocytes and stem cells involved in mediating the inflammatory cascade. Mutations and deletions in the gene encoding Alpha-2M are associated with an increased incidence of Alzheimer s disease (AD), which is consistent with the role of Alpha-2M in mediating the clearance and degradation of A beta, the major component of beta-Amyloid deposits accumulated during AD. Protein function: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. [The UniProt Consortium]