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Immunoglobulin E (IgE) is a type of antibody (or immunoglobulin (Ig) "isoform") that has been found only in mammals. IgE is synthesised by plasma cells. Monomers of IgE consist of two heavy chains (ε chain) and two light chains, with the ε chain containing four Ig-like constant domains (Cε1–Cε4). [1]
An IgE level greater than 2,000 IU/mL is often considered diagnostic. [17] However, patients younger than 6 months of age may have very low to non-detectable IgE levels. Eosinophilia is also a common finding with greater than 90% of patients having eosinophil elevations greater than two standard deviations above the normal mean. [ 18 ]
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain.
The IgG, IgE and IgA antibody isotypes are generated following class-switching during germinal centre reaction and provide different effector functions in response to specific antigens. IgG is the most abundant antibody class in the serum and it is divided into 4 subclasses based on differences in the structure of the constant region genes and ...
The RAST is a radioimmunoassay test to detect specific IgE antibodies to suspected or known allergens for the purpose of guiding a diagnosis about allergy. [10] [11] IgE is the antibody associated with Type I allergic response: for example, if a person exhibits a high level of IgE directed against pollen, the test may indicate the person is allergic to pollen (or pollen-like) proteins.
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Atopy is the tendency to produce an exaggerated immunoglobulin E (IgE) immune response to otherwise harmless substances in the environment. [2] Allergic diseases are clinical manifestations of such inappropriate, atopic responses.
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