Also known as the ELISA, the process of enzyme-linked immunosorbent assay is a popular format of analytic biochemisty assay that uses a single subtype of heterogeneous solid-phase enzyme immunoassay (also known as EIA) to detect the presence of an antigen (or a specific substance) in a wet or liquid sample.
The enzyme-linked immunosorbent assay is typically used as a diagnostic tool in medicine and plant pathology, and a quality-control checking method in various industries that involve biochemistry. The process of enzyme-linked immunosorbent assay entails the attempt to both detect and quantify the presence of an antigen in a sample by following a specific set of steps. First, the antigens from the sample are attached to a surface. A further specific antibody will then be applied over the surface to help it bind to the antigen. The antibody used in the process is linked to an enzyme, and in the final step of the process, to a substance with the enzyme’s substrate. The process will result to a subsequent reaction, which produces a detectable signal—typically a color change in the enzyme’s substrate that was added in the final step.
There are different types of enzyme-linked immunosorbent assay: the indirect, the sandwich, multiple and portable, and the competitive ELISA. These types of assay processes can be used for various purposes, and are typically available in kits that are relatively easy to use.
The ELISA can also be used to detect and evaluate the process of an antibody in the sample, which means that it can be used to determine serum antibody concentrations in tests for the HIV or the West Nile Virus. Food industries also rely in this test to detect potential allergens in items such as milk, peanuts, almonds, eggs, and walnuts.
This category contains scientific information of the enzyme-linked immunosorbent assay, a type of test that determines the antigen and antibody concentration in a certain sample.
Toft D.O., 1986: Preparation of monoclonal antibodies to the avian progesterone receptor. Endocrinology: 1549-1557 In an effort to obtain additional probes for analysis of the avian progesterone receptor, this receptor was isolated and used to prepare several monoclonal antibodies. Progesterone receptor purified from oviduct cytosol by chromatography on deoxycorticosterone-Separose and heparin-agarose was used as the [...]
Glimcher M.J., 1988: Preparation of monoclonal antibodies to chicken bone phosphoproteins. Calcified Tissue International: 41-43 Monoclonal and polyclonal antibodies were raised against 150k, 60k, 32k, and 15k phosphoprotein components of 14-week chicken bone. Hybridomas were prepared by immunizing Balb/c mice with 150k, 60k, or 32k phosphoproteins followed by fusion of their spleen cells with X63-Ag8.653 [...]
Iwata D., 1987: Preparation of monoclonal antibodies against a glycolipid asialo gm1. Microbiology & Immunology: 923-934 Five IgM monoclonal antibodies (MAbs), Mw-1, Mw-2, Mw-3, Mw-4, and Mw-5, against a glycolipid asialo Gm1 were prepared from hybridoma clones obtained by the fusion of mouse Ns-1 myeloma cells with spleen cells from a mouse immunized with asialo [...]
Stoltz J.F., 1984: Preparation of intravenous cytomegalovirus immune globulin. Revue Francaise De Transfusion Et Immuno Hematologie: 383-390 Immune plasmas were selected from 3640 healthy volunteer blood donors on the basis of complement fixation (Cf) antibody titers to cytomegalovirus (Cmv) of at least 1:8; plasmas from.apprx. 10% of the donors were therefore selected. The 68 l [...]
Ito, K.; Katayama, M.; Minamiura, N.; Yamamoto, T., 1985: Preparation of human salivary alpha amylase ec 188.8.131.52 specific monoclonal antibody. Journal of Biochemistry (Tokyo) 97(5): 1357-1362 A mouse hybridoma cell line which produced an anti-human salivary.alpha.-amylase monoclonal antibody was obtained by fusion between mouse spleen cells immunized with human salivary.alpha.-amylase and mouse myeloma cells, followed [...]
Yachi A., 1986: Preparation of human monoclonal antibodies of immunoglobulin g type to gastro intestinal cancer associated antigen. Japanese Journal Of Cancer Research: 722-729 The B lymphocytes from pleural effusion of a gastric cancer patient were fused with murine myeloma cells (X63-Ag8.653). Thirty-four out of 62 clones were found to secrete human monoclonal antibodies (23 [...]
Kishida T., 1985: Preparation of anti gm antibodies and their application to elisa and immunoblotting for gm typing. Japanese Journal Of Human Genetics: 201-212 Gm typing has not yet come into widespread use in forensic science practice because of the short supply of anti-Gm sera and anti-Rho sera indispensable for the conventional hemagglutination-inhibiiton method. To [...]
Swanepoel R., 1987: Preparation and use of monoclonal antibodies for identifying crimean congo hemorrhagic fever virus. American Journal Of Tropical Medicine & Hygiene: 392-397 Seven monoclonal antibodies were prepared against a South African strain of Crimean-Congo hemorrhagic fever (Cchf) virus and were found to be directed against viral nucleocapsid protein. Five of the monoclonal antibodies [...]
Rapport M.M., 1986: Preparation and specificity of 11 monoclonal antibodies to g m 1 ganglioside. Journal Of Neurochemistry: 1172-1175 Eleven monoclonal antibodies to Gm1 ganglioside were prepared from hybridoma clones obtained by fusion of spleen cells from mice immunized with Gm1 with mouse myeloma cells. When the reactivities of these 11 monoclonal antibodies were deterined [...]
Dankert J., 1980: Preparation and quantitative determination of antibodies against major outer membrane proteins of escherichia coli o 26 k 60. Journal Of General Microbiology: 437-448 Antisera against isolated outer membrane (Om) proteins I and Ii* of E. coli O26 K60 were elicited in rabbits. Antisera obtained after i.m. administration with Freund’s complete adjuvant showed [...]