A portion of amino acids 604-748 from the human protein was used as the immunogen for the Alpha-2-Macroglobulin antibody.
Alpha-2-Macroglobulin (A2M) is a homotetrameric serum protein consisting of four identical subunits that form dimers through disulfide bonds. Initially, it was characterized as a pan-proteinase inhibitor that was able to bait proteinases into cleaving specific peptide sequences on A2M. This interaction induces a conformational change, thus enabling it to trap the proteinase and further inhibit its activity. Subsequently, A2M has been shown to function as a carrier protein and regulator of cytokines during inflammation.