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Crossed immunoelectrophoresis of 2 microlitres of normal human serum. The electrophoresis was performed in thin layers of agarose; the pictured gel is about 7x7 cm. The lower part is the first dimension gel without antibodies, where the serum was applied into the slot at the lower left.
The principles of specificity and cross-reactivity of the antigen-antibody interaction are useful in clinical laboratory for diagnostic purposes. One basic application is determination of ABO blood group. It is also used as a molecular technique for infection with different pathogens, such as HIV, microbes, and helminth parasites.
Immunofixation as immunoelectrophoresis, takes place in two steps: The first step is identical for both techniques. It consists in depositing the immunoglobulins contained in the serum or urine on a gel and then separating the immunoglobulins according to their electrophoretic mobility by making them migrate under the effect of an electric field.
Plasmodium Glutamate dehydrogenase (pGluDH) separated by counterimmunoelectrophoresis [1]. Counterimmunoelectrophoresis is a laboratory technique used to evaluate the binding of an antibody to its antigen, it is similar to immunodiffusion, but with the addition of an applied electrical field across the diffusion medium, usually an agar or polyacrylamide gel.
Immunochemical techniques include: enzyme-linked immunosorbent assay, immunoblotting (e.g., Western blot assay), precipitation and agglutination reactions, immunoelectrophoresis, immunophenotyping, immunochromatographic assay and cyflometry. One of the earliest examples of immunochemistry is the Wasserman test to detect syphilis.
Proteins separated by SDS-PAGE, Coomassie brilliant blue staining. Protein electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium, namely agarose or polyacrylamide.
When more than one well is used there are many possible outcomes based on the reactivity of the antigen and antibody selected. The zone of equivalence lines may give a full identity (i.e. a continuous line), partial identity (i.e. a continuous line with a spur at one end), or a non-identity (i.e. the two lines cross completely). [citation needed]
In 1953 Grabar developed immunoelectrophoresis, combining electrophoresis and immunochemical analysis to create an "immuno-electrophoretic method". [24] He used a gel medium, designed by Jacques Oudin, also at the Institut Pasteur, and developed the immunoelectrophoretic analysis method with the help of American student Curtis A. Williams, Jr ...