Human a2ML1(Alpha-2-Macroglobulin Like Protein 1) ELISA Kit

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 Assay Type: Sandwich. Sensitivity: 0.066 µg/mL. Standard: 10 µg/mL. Detection range: 0.16-10 µg/mL. Sample type: serum, plasma, tissue homogenates and other biological fluids. Assay length: 3.5h. Research Field: Infection immunity,. Test principle: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human a2ML1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human a2ML1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human a2ML1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human a2ML1 in the samples is then determined by comparing the OD of the samples to the standard curve.