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Alpha-2-macroglobulin-like protein

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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). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.

Below are the list of possible Alpha-2-macroglobulin-like protein products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Alpha-2-macroglobulin-like protein 1

 Alpha-2-macroglobulin-like protein 1 ELISA Kit
 Alpha-2-macroglobulin-like protein 1 Recombinant
 Alpha-2-macroglobulin-like protein 1 Antibody
Also known as Alpha-2-macroglobulin-like protein 1 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9).
A2ML1: 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 conformationa
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l 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. Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases. Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family.

Protein type: Inhibitor; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 12p13.31

Cellular Component: extracellular space

Molecular Function: protease inhibitor activity

Biological Process: regulation of endopeptidase activity
 A2ML1 ELISA Kit
 A2ML1 Recombinant
 A2ML1 Antibody
 CPAMD9 ELISA Kit
 CPAMD9 Recombinant
 CPAMD9 Antibody
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