Human Immunoglobulin E, Lambda (IgE M Lambda)
Native whole molecule protein, purified from myeloma plasma
Produktdetails
Synonyms
IgE-L Myeloma
Description of Human Immunoglobulin E, Lambda (IgE M Lambda)
Human Immunoglobulin E, Lambda (IgE M Lambda) is a 190 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 myeloma 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, Lambda (IgE M Lambda) at ≤ -80°C.
Applications
Allergy, Aptamer, Glycoproteomics, In Vitro Diagnostic, Inflammation, Biosensors, ELISA Standards, Parasitic Infections.
Citations/Publications
Canoura, J., et al., (2021), 'Accelerating Post-SELEX Aptamer Engineering Using Exonuclease Digestion', J Am Chem Soc., 143(2): pp 805–816. Available at: doi:10.1021/jacs.0c09559.
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. Available at: https://doi.org/10.1155/2018/2136193
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. Available at: http://dx.doi.org/10.1016/j.bbapap.2015.08.008
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. Availablae at: https://doi.org/10.4049/jimmunol.2100485
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. Available at: DOI: 10.1007/s13361-015-1308-6
Shipped with dry ice
Gel Scan of Human Immunoglobulin E, Lambda (IgE M Lambda)
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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