Enzyme-Linked ImmunoSorbent Assay (ELISA): 35 Years After
Filed in archive Diagnostics, Methodologies and Instrumentation by ruth on May 22, 2006

, such as those making up cellular components of bacteria and viruses, in solutions such as serum, urine, or culture media. Aside from detecting pathogens, the ELISA has also been adapted to detect food allergies, particularly for the treatment of Irritable Bowel Syndrome.How does it work? Here's how the general method runs, as described in Wikipedia:
- Apply a sample of known antigen to a surface, often the well of a microtiter plate. The antigen is fixed to the surface to render it immobile.
- The plate wells or other surface are then coated with serum samples of unknown antibody concentration, usually diluted in another species' serum. The use of non-human serum prevents non-specific antibodies in the patient's blood from binding to the antigen.
- The plate is washed, so that unbound antibody is removed. After this wash, only the antibody-antigen complexes remain attached to the well.
- The second antibodies are added to the wells, which will bind to any antigen-antibody complexes. These second antibodies are coupled to the substrate-modifying enzyme.
- Wash the plate, so that excess unbound antibodies are removed.
- Apply a substrate which is converted by the enzyme to elicit a chromogenic or fluorescent signal.
- View/quantify the result using a spectrophotometer or other optical device.
If you want to know more about oen of its discoverers, Eva Engvall, Joe Palca from National Public Radio has written a feature story.
Permalink: Enzyme-Linked ImmunoSorbent Assay (ELISA): 35 Years After
Tags:
ELISA diagnostics biotech elisa enzyme enzyme+linked assay+elisa immunosorbent+assay
Trackback: http://www.creative-weblogging.com/cgi-bin/mt-tb.pl/22443





