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Human Immunoglobulin E (IgE)
Native whole molecule protein, purified from multiple donor pool
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Proteine Synonyms: IgE Source: Human Plasma Purity: ≥ 95% by SDS-PAGE Physical State: Frozen in 100 mM Tris, pH 7.5, with 200 mM NaCl and 0.05% sodium azide. Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
IgE
Description of Human Immunoglobulin E (IgE)
Human Immunoglobulin E (IgE) is a 200 kDa protein. Serum immunoglobulin E (IgE) is the least abundant antibody class in human plasma, circulating at concentrations below 0.6 µg/mL in healthy individuals. This monomeric glycoprotein features a unique Fc region with seven N-linked glycosylation sites, including a conserved oligomannose glycan at Asn394 critical for structural stability and binding to the high-affinity receptor FcεRI. IgE mediates type I hypersensitivity reactions by binding FcεRI on mast cells and basophils, triggering degranulation and release of histamine, leukotrienes, and cytokines upon allergen exposure. Beyond allergies, IgE plays a protective role against parasitic infections like helminths by activating eosinophils and basophils to release cytotoxic granules. Elevated serum IgE (>300 IU/mL) is a hallmark in allergic conditions such as asthma, atopic dermatitis, and allergic bronchopulmonary aspergillosis (ABPA). Hyperimmunoglobulinemia E syndromes (HIES), caused by STAT3 mutations, present with recurrent infections, eczema, and IgE levels exceeding 2, 000 IU/mL. IgE multiple myeloma, a rare plasma cell malignancy, produces monoclonal IgE with normal structure but lambda light chain predominance, often complicating renal function. Parasitic infections and viral diseases like HIV also drive polyclonal IgE elevation. Clinically, total IgE quantification aids in diagnosing ABPA and monitoring omalizumab therapy, an anti-IgE monoclonal antibody that reduces free IgE levels by forming inert complexes. Despite its short serum half-life (2–3 days), cell-bound IgE persists for weeks on immune cells, necessitating combined plasma and cell-bound IgE measurements for accurate allergy diagnosis. Myeloma-derived IgE remains invaluable for structural studies due to its intact glycosylation and receptor-binding properties. Emerging therapies targeting IgE-FcεRI interactions and glycosylation pathways aim to modulate allergic responses while preserving protective functions.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human Immunoglobulin E (IgE) at ≤ -80°C.
Applications
Allergy, Aptamer, Glycoproteomics, In Vitro Diagnostic, Inflammation, Biosensors, ELISA Standards, Parasitic Infections.
Citations/Publications
Achille, C., et al., (2021), '3D Printing of Monolithic Capillarity-Driven Microfluidic Devices for Diagnostics', Adv. Mater. 33: 2008712. Available at: https://doi.org/10.1002/adma.202008712
Wang, L., et al., (2019), 'A DNA aptamer for binding and inhibition of DNA methyltransferase 1', Nucleic Acids Research, 47(22): pp 11527–11537. Available at: doi: 10.1093/nar/gkz1083
Zhu, F., et al., (2024), 'CRISPR/Cas12a powered sandwich aptamer assay coupled with effective DNA self-assembly amplification for sensitive detection of immunoglobulin E', Sensors & Actuators: B. Chemical 422: pp 136615. Available at: https://doi.org/10.1016/j.snb.2024.136615
Wang, X., et al., (2019), 'Measurements of aptamer-protein binding kinetics using graphene field-effect transistors', Nanoscale., 11(26): pp 12573-12581. Available at: doi: 10.1039/c9nr02797a.
Liu, Y. M., et al., (2016), 'An electrochemiluminescence aptasensor based on CdSe/ZnS functionalized MoS2 and enzymatic biocatalytic precipitation for sensitive detection of immunoglobulin E.', Sensors and Actuators B 232: pp 538–544. Available at: https://doi.org/10.1016/j.snb.2016.03.165
Shipped with dry ice
Gel Scan of Human Immunoglobulin E (IgE)
| Fig. 1: SDS-PAGE Gel |
Verwendung: Nur für Forschungszwecke. Nicht zur Verwendung in diagnostischen oder therapeutischen Verfahren. Nicht für den menschlichen Gebrauch.
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