- {{heading}}
- Ab00874-10.17 Anti-IgE [rhuMAb-E25 (Omalizumab)]
- Human
- Human IgG1
- -
- In Stock
Recombinant monoclonal antibody to IgE. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma rhuMAb-E25 (Omalizumab).
UniProt Accession Number of Target Protein: P12319
Alternative Name(s) of Target: Immunoglobulin epsilon; FcERI; FCER1; FCϵRI; FCϵR1; Fc-epsilon RI-alpha; IgE Fc receptor subunit alpha
Immunogen: The original antibody is the recombinant humanized version of MaE11, a murine anti-IgE monoclonal antibody, constructed from the complementarity determining regions of MaE11 and a human IgG1 frame.
Specificity: This antibody is specific for the Fc region of human IgE.
Application Notes: This antibody has two potential binding sites on IgE (one for each Fc heavy chain) and, therefore, can function as a multivalent ligand that complexes with IgE in various conformations depending on the ratio of their molar concentrations (Liu et al., 1995; PMID: 7654701). This antibody has been shown to reduce serum IgE levels and significantly attenuate both the early- and late-phase responses to inhaled allergen in allergic asthmatic subjects (Fahy et al., 1997; PMID: 9196082). Omalizumab treatment has been shown to reduce asthma exacerbations and decrease inhaled corticosteroid and rescue medication use in the treatment of severe allergic asthma (Busse et al., 2001; PMID: 11496232). The therapeutic product made using this antibody (omalizumab) binds to human IgE in blood or membrane-bound IgE on B lymphocytes. Furthermore, omalizumab competes with IgE's high and low-affinity receptors — FcεRI and CD23, respectively — for binding to residues in the CH3 domain. Therefore, it effectively blocks human IgE binding to FcϵRI without stimulating the degranulation of mast cells and basophils, i.e., without triggering a severe, life-threatening anaphylactic reaction (Wright et al., 2015; PMID: 26113483).
Antibody first published in:
Liu et al. Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE Biochemistry. 1995 Aug 22;34(33):10474-82. doi: 10.1021/bi00033a020 PMID:7654701
Note on publication:
The original publication characterizes the formation of immune complexes between a humanized anti-IgE monoclonal antibody and IgE, revealing various complex structures and a high-affinity interaction.