ELISA is an abbreviation for "enzyme-linked immunosorbent assay."
Enzyme immunoassays were first reported in 1971 by S. Avrameas and B. Guilbert in France, E. Engvall and P. Perlmann in Sweden, and B. van Weemen and H. Schuurs in Holland. They were employed for the quantitation of antigens and subsequently for the titration of antibodies.
ELISA is a technique used to detect the presence of an antibody or antigen in a variety of samples. There are several different types of ELISAs including indirect, sandwich, competitive, and reverse ELISAs. All of these can be used to detect proteins, viruses, and drugs.
There are four types or kinds of ELISA tests:
1) Direct ELISA 2) Indirect ELISA 3) Sandwich ELISA and 4) Competitive ELISA.
Performing an ELISA involves at least one antibody with specificity for a particular antigen. The sample with an unknown amount of antigen is immobilized on a solid support (usually a polystyrene microtiter plate, see in detail in the section of ELISA device) either non-specifically (via adsorption to the surface) or specifically (via capture by another antibody specific to the same antigen, in a "sandwich" ELISA). After the antigen is immobilized, the detection antibody is added, forming a complex with the antigen. The detection antibody can be covalently linked to an enzyme, or can itself be detected by a secondary antibody that is linked to an enzyme through bioconjugation. The part of antibody incubation of ELISA is similar with that of western blot. Between each step, the plate is typically washed with a mild detergent solution to remove any proteins or antibodies that are not specifically bound. After the final wash step, the plate is developed by adding an enzymatic substrate to produce a visible signal, which indicates the quantity of antigen in the sample.
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