| Product Name | Human Alpha-2-macroglobulin-like protein 1 (A2ML1) ELISA Kit |
|---|---|
| Description | The alpha-macroglobulin (AM) superfamily of proteins contains both complement components and protease inhibitors, including A2M and A2ML1. AM proteins display a unique trap mechanism of inhibition, by which the AM inhibitor undergoes a major conformational change upon its cleavage by a protease, thus trapping the protease and blocking it from subsequent substrate binding. 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. Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. This assay has high sensitivity and excellent specificity for detection of Human A2ML1. No significant cross-reactivity or interference between Human A2ML1 and analogues was observed. |
| Synonyms | CPAMD9, DKFZp686C1729, DKFZp686D2011, DKFZp686G1812, DKFZp686L1821, DKFZp686O1010, FLJ16045, FLJ25179, FLJ39129, FLJ41597, FLJ41598, FLJ41607, C3 and PZP-like, alpha-2-macroglobulin domain containin |
| Method | Sandwich ELISA |
| Detection Range | 0.78-50 ng/mL |
| Sensitivity | 0.34 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | The alpha-macroglobulin (AM) superfamily of proteins contains both complement components and protease inhibitors, including A2M and A2ML1. AM proteins display a unique trap mechanism of inhibition, by which the AM inhibitor undergoes a major conformational change upon its cleavage by a protease, thus trapping the protease and blocking it from subsequent substrate binding. 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. Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. |
| Supplier | Abebio |
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