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Alpha-2-macroglobulin

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 (By similarity).

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Alpha-2-macroglobulin

Also known as Alpha-2-macroglobulin (Alpha-2-M).
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 ().

Alpha-2-macroglobulin-P

Also known as Alpha-2-macroglobulin-P (Alpha-2-macroglobulin).
A2M: 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. Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family.

Protein type: Inhibitor; Secreted; Secreted, signal peptide

Cellular Component: extracellular space

Molecular Function: brain-derived neurotrophic factor binding; calcium-dependent protein binding; endopeptidase inhibitor activity; enzyme binding; growth factor binding; interleukin-1 binding; interleukin-8 binding; nerve growth factor binding; protease binding; protease inhibitor activity; protein binding; protein homodimerization activity; receptor binding; serine-type endopeptidase inhibitor activity; tumor necrosis factor binding

Biological Process: negative regulation of complement activation, lectin pathway; stem cell differentiation

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