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.

Protein names

Recommended name:

Alpha-2-macroglobulin

Alternative name(s):

Alpha-2-M
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5

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Top Gene-Substance Interactions

A2M Interacts with These Diseases

Substances That Increase A2M

Substances That Decrease A2M

Conditions with Increased Gene Activity

Conditions with Decreased Gene Activity

Technical