Immunoglobulin E, Lambda
16-16-090705-M-Lambda
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Research
- Product NameImmunoglobulin E, Lambda
- Delivery Days Customer9
- Applications SupplierAllergy, Aptamer, Glycoproteomics, In Vitro Diagnostic, Inflammation, Biosensors, ELISA Standards, Parasitic Infections
- CertificationResearch Use Only
- Estimated Purity≥95% by SDS-PAGE
- Scientific DescriptionSerum immunoglobulin E (IgE) is the least abundant antibody class in human plasma, circulating at concentrations below 0.6 ug/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 FcepsilonRI. IgE mediates type I hypersensitivity reactions by binding FcepsilonRI 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 (more then300 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-FcepsilonRI interactions and glycosylation pathways aim to modulate allergic responses while preserving protective functions.
- Shelf life instructionmore then 1 year
- SourceSource human myeloma plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
- Storage Instruction≤ -80° C
- UNSPSC41116100
References
- Canoura, J., et al., (2021), 'Accelerating Post-SELEX Aptamer Engineering Using Exonuclease Digestion', J Am Chem Soc., 143(2): pp 805–816.Read this paper
- Derakhshan, T., et al., (2018), 'Development of Human Mast Cells from Hematopoietic Stem Cells within a 3D Collagen Matrix: Effect of Stem Cell Media on Mast Cell Generation', Stem Cells International., Vol. 2018, Article ID 2136193, 14 pages.Read this paper
- Poongavanam, M. V., et al., (2016), 'Ensemble and Single-Molecule Biophysical Characterization of D17.4 DNA Aptamer-IgE Interactions', Biochimica et Biophysica Acta 1864: pp 154–164.Read this paper
- Adnan, A., et al., (2023), 'Multistep IgE Mast Cell Desensitization Is a Dose- and Time-Dependent Process Partially Regulated by SHIP-1', The Journal of Immunology, 210: pp 709-720.Read this paper
- Hinneburg, H., et al., (2016), 'The Art of Destruction: Optimizing Collision Energies in Quadrupole-Time of Flight (Q-TOF) Instruments for Glycopeptide-Based Glycoproteomics', J. Am. Soc. Mass Spectrom., 201 (27): pp 507-519.Read this paper