Specificity: Apis mellifera hyaluronidase (allergen Api m 2)
Epitope: Sequence RREHPFWDDQR
Application: ELISA
Multiplex assay ready: PBS only formulation, ready for custom conjugation.
Summary
Specifications
Antibody Isotype
IgG
Clone
21E11
Species Reactivity
Apis mellifera
Immunogen
Recombinant Api m 2, a major bee venom allergen.
Conjugate
Unconjugated
Applications
Application Notes
Suitable for use in ELISA. Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
General Notes
The major allergens of honeybee venom, hyaluronidase (Hyal) and phospholipase A2, can induce life-threatening IgE-mediated allergic reactions in humans. Although conventional immunotherapy is effective, up to 40% of patients develop allergic side effects including anaphylaxis and thus, there is a need for an improved immunotherapy. A monoclonal anti-Hyal IgG1 antibody (clone 21E11), that competed for Hyal binding with IgEs from sera of bee venom allergic patients, was raised. The fragment of these IgG antibodies which bind to antigen (Fab) was produced and complexed (1:1) with Hyal. The crystal structure determination of Hyal/Fab 21E11 complex (2.6 A) enabled the identification of the Hyal-IgG interface which provides indirect information on the Hyal-IgE interaction (B-cell epitope). The epitope is composed of a linear array of nine residues (Arg138, His141-Arg148) located at the tip of a helix-turn-helix motive which protrudes away from the globular core and fits tightly into the deep surface pocket formed by the residues from the six complementarity determining regions (CDRs) of the Fab. The epitope is continuous and yet its conformation appears to be essential for Ab recognition, since the synthetic 15-mer peptide comprising the entire epitope (Arg138-Glu152) is neither recognized by mAb 21E11 nor by human IgEs. The structure of the complex provides the basis for the rational design of Hyal derivatives with reduced allergenic activity, which could be used in the development of safer allergen-specific immunotherapy.
Target
Alternative Names
Hyaluronidase; Bee venom allergen; Hyaluronidase; Hya; Hyal; Api m II; Bee venom allergens phospholipase; Hyaluronidase; Melittin; Api m 2
Citations
Publication ()
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