Human alpha-2-macroglobulin (His Tag) recombinant protein
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 short names
A2MD; S863-7; CPAMD5; A2M; FWP007; ALPHA-2-MACROGLOBULIN; A2MP; DKFZP779B086
A2M; CPAMD5; FWP007
A DNA sequence encoding the human A2M (NP_000005.2) (Met 1-Ala 1474) was expressed, fused with a polyhistidine tag at the C-terminus.
The recombinant human A2M consists of 1461 amino acids and predicts a molecular mass of 164 kDa. The apparent molecular mass of rhA2M is approximately 160-170 kDa in SDS-PAGE under reducing conditions.
> 92 % as determined by SDS-PAGE
Measured by its ability to trap trypsin. The trapped trypsin is no longer able to interact with protein substrates or inhibitors, but still able to cleave small peptide substrates or inhibitors.
The IC50 value is <5 nM.
Human A2M / CPAMD5 / Alpha-2-macroglobulin Protein (His Tag) SDS-PAGE
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