Human IgE抗体—艾普蒂

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     100 ng of human IgE was run on 6-18% SDS-PAGE under reducing conditions and blotted onto nitrocellulose membrane. P16113 at 1 µg/mL was used as the primary antibody and peroxidase conjugated goat anti-mouse IgG was used as the secondary antibody. Human IgE band was visualized using ECL Substrate. Result: P16113 can detect human IgE by Western blotting.    

  
  

Human immunoglobulin E (IgE) is a key antibody isotype involved in type I hypersensitivity reactions and allergic responses. Discovered in 1967. IgE has a characteristic structure comprising two heavy chains (ε-chains) and two light chains, with a high-affinity Fc region binding to FcεRI receptors on mast cells and basophils. Unlike other immunoglobulins, IgE exists at very low concentrations in serum (nanograms per milliliter) under normal conditions but increases dramatically during allergic disorders or parasitic infections.

Its primary biological role involves host defense against helminths and certain protozoan parasites by triggering mast cell degranulation and eosinophil activation. However, in allergic individuals, IgE mistakenly recognizes harmless antigens (allergens) like pollen or food proteins, leading to cross-linking of FcεRI-bound IgE molecules. This activates effector cells to release histamine, leukotrienes, and cytokines, causing immediate symptoms (itching, bronchoconstriction) and late-phase inflammation.

Clinically, serum IgE levels are measured to assess allergic conditions (asthma, atopic dermatitis) and parasitic infections. Allergen-specific IgE testing forms the basis of diagnostic tools like RAST tests. Therapeutic strategies targeting IgE include anti-IgE monoclonal antibodies (e.g., omalizumab) that block FcεRI binding, as well as allergen immunotherapy to modulate IgE production. Recent research explores IgE's role in cancer immunosurveillance and autoimmune diseases, expanding its clinical significance beyond classical allergy paradigms.