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DIA HE1-01 contains purified human IgE with kappa light chains produced in vitro from a monoclonal hybridoma. Original material is obtained from a healthy donor tested negative by US-FDA approved tests against HIV, HCV and Hepatitis B, but must be handled as potentially infectious, as should all human material.
The purity of this human IgE is >98%, tested by SDS-PAGE. As the IgE comes from a monoclonal cell line, there is no contamination of antibodies of other isotypes. The human IgE is purified by Protein L chromatography. The remaining contaminants are mainly components from Foetal Bovine Serum.
This antibody is well suited as a standard in IgE quantifying assays due to its very low batch-to-batch variation. Other applications include immunochemistry and cellular immunology research.
NOTE: Concentration is lot-dependent and can vary from 0.85-1.15 mg/mL
IgE is one of the five classes of immunoglobulins found in mammals, characterized by its monomeric structure consisting of two heavy (epsilon) chains with four Ig-like constant domains and two light chains. Although IgE comprises only a small portion of the total immunoglobulin in serum, it plays a crucial role in type I hypersensitivity reactions, such as hay fever, asthma, hives, and anaphylactic shock. IgE is produced by terminally differentiated plasma B cells and basophils. It binds to Fc epsilon receptors on mast cells and basophils, leading to the release of histamine and other molecules that promote allergic responses. Crosslinking of IgE bound to these receptors induces degranulation of mast cells and basophils, resulting in allergic manifestations. In addition to its role in allergic responses, IgE is functionally important for immunity against parasites, highlighting its dual role in both protective and pathological immune processes.
仅用于科研。不用于诊断过程。未经明确授权不得转售。