A recombinant partial protein sequence (within amino acids 600-800) from the human protein was used as the immunogen for the Alpha-2-Macroglobulin antibody.
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.
