alpha-2-Macroglobulin Polyclonal Antibody – Affinity Purified – HRP Conjugated
Affinity’s alpha-2-Macroglobulin Polyclonal Antibody – Affinity Purified – HRP Conjugated is the highest level of our horseradish peroxidase conjugated alpha-2-Macroglobulin antibodies. During the Antigen Affinity Purification process the IgG has had any non-specific immunoglobulin fraction eliminated which enriches the specificity of the remaining immunoglobulin towards the target antigen. The result is a very high-purity product with a substantially higher titre than whole or purified IgG. Our alpha-2-Macroglobulin Polyclonal Antibody – Affinity Purified – HRP Conjugated is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v) and has been conjugated with Horseradish Peroxidase as an enzyme reporter. This antibody is generally intended for use as labeled primary antibodies in applications such as immunoassay and immunoblotting.
Description of Alpha 2-Macroglobulin
Alpha 2-Macroglobulin (A2M) is a large proteinase inhibitor molecule of 718,000 daltons, consisting of 4 identical subunits of 185,000 each. Produced in hepatocytes and macrophages, plasma concentrations of A2M are typically 2 uM in adults, and as high as 6 uM in childhood. A2M has the ability to inhibit most enzymes from the serine, metallo, cysteine and aspartate subclasses. It is not a member of the SERPIN family of inhibitors but belongs to a class of proteins that include pregnancy zone protein (PZP) and the complement proteins C3, C4 and C5. These proteins contain regions of conserved sequence as well as one or more internal beta-cysteinyl-gamma-glutamyl thiolester bonds, which in the case of A2M are susceptible to cleavage by enzymes or by nucleophilic compounds such as methylamine or ammonium ions. Although the precise nature of the interactions is as yet unknown, it is generally thought that cleavage of a bait region within the A2M molecule by an enzyme leads to a conformational change, which then traps and/or covalently binds the enzyme1,2. The active site of the trapped enzyme is usually still intact and able to cleave small substrates, but is inaccessible to larger natural substrates. The conformational change induced also exposes receptor-binding regions within the molecule, which may be important in the clearance of A2M-enzyme complexes from the circulation. It is thought that the main role of A2M in vivo is that of a “backup” inhibitor and scavenger of proteinases in blood and in tissues3,4, but it has also been reported to participate in other physiological processes, including regulation of immune function1,2.