Description
Intended Uses: This DGP-IgA ELISA is a solid phase enzyme immunoassay employing synthetic, deamidated gliadin-derived peptides for the quantitative and qualitative detection of IgA antibodies against deamidated Gliadin-specific peptides (DGP) in human serum.
Principle of the Assay: Serum samples diluted 1:101 are incubated in the microplates coated with the specific antigen. The antibodies, if present in the specimen, bind to the antigen. The unbound fraction is washed off in the following step. Afterwards anti-human immunoglobulins conjugated to horseradish peroxidase (conjugate) are incubated and react with the antigen-antibody complex of the samples in the microplates. Unbound conjugate is washed off in the following step. Addition of TMB-substrate generates an enzymatic colorimetric (blue) reaction, which is stopped by diluted acid (color changes to yellow). The intensity of color formation from the chromogen is a function of the amount of conjugate bound to the antigen-antibody complex and this is proportional to the initial concentration of the respective antibodies in the sample.
Background: Gluten-sensitive enteropathy or celiac disease is characterized by atrophy of the small intestinal villi leading to a so-called flat mucosa. It is caused by a pathological intolerance to Gliadin, the alcohol-soluble fraction of gluten in wheat, rye and barley. As celiac disease is caused by the uptake of gluten, consequently a gluten-free diet cures the disease completely and thus has to be maintained for life-time. Renewed consumption of Gliadin leads to a return of the symptoms. The disease is HLA-associated (>95% of individuals have DQ2 enREFd by DQA1*0501 and DQB1*0201) and manifests at any age with a peak onset in early childhood, even in neonatals. The incidence rates range from 1 in 4000 to 1 in 300 in European countries