Immunoassays are a very important tool in bioanalytical and biochemical laboratories. They are used in research, food and environmental monitoring as well as in diagnostic applications. Immunoassays are quite easy to carry out and very specific in terms of quantitative and qualitative significance due to their use of antibodies for detection. Theoretically, each antibody can identify one antigen and binds this antigen with high affinity which explains why one can distinguish so easily between different substances.
In practice, it is not that simple. Although antibodies are very specific and have high affinity for one antigen in particular, often antibodies can also bind with lower affinity to other antigens which are not detected by the assay. This is even observed with very well characterised antibodies known to have a high affinity to the target analyte. Immunoassays suffer from cross reactivity which results in false bands in Western blots, signals in the negative control of an ELISA or a very high background in a protein array. Every false result means more work, additional costs and potentially misdiagnosis of patients.
There are several types of these assays including Enzyme linked immunosorbent assays (ELISA), enzyme immunoassays (EIA), Western blotting, radioactive labelled immunoassays (RIA), protein arrays, immunohistochemistry, and immunopolymerasechain reaction (ImmunoPCR). And each of these assays have one drawback in common cross reactivity!
This brochure provides a survey on getting most of these drawbacks under control. To learn more about •Non-specific binding, •Cross reactivity, •Matrix effects, •Anti-Animal-Antibodies, •Heterophilic antibodies, •Interference caused by endogenous components of the specimen, and, how to •Avoiding the interference by applying novel immunoassay buffers download our brochure.