IGHE Recombinant Monoclonal Antibody

Immunoglobulin heavy constant epsilon (IGHE) forms the constant region of IgE antibodies, the least abundant immunoglobulin class in circulation yet one of the most biologically potent. IgE plays a central role in type I hypersensitivity reactions, allergic responses, and defense against parasitic infections. The epsilon heavy chain determines IgE's unique ability to bind high-affinity FcεRI receptors on mast cells and basophils, triggering degranulation upon allergen crosslinking. This makes IGHE a critical target for researchers investigating allergic disease mechanisms, asthma pathophysiology, and novel therapeutic approaches targeting the IgE pathway.

This recombinant monoclonal antibody, clone 11D7, offers the reproducibility essential for longitudinal studies and multi-site collaborations. Because recombinant antibodies are produced from defined sequences rather than hybridoma supernatants, you can expect consistent performance across lots, eliminating the variability that can compromise experimental comparisons over time. The antibody is supplied in human IgG1 format and has been affinity-purified to ensure high specificity for human IGHE.

Functional ELISA validation demonstrates robust binding activity, with immobilized human IGHE protein detected at EC50 values ranging from 3.097 to 4.487 ng/mL, indicating excellent sensitivity at recommended dilutions between 1:5000 and 1:50000. This broad working range provides flexibility for optimizing signal-to-noise ratios across different experimental setups.

This antibody supports research into IgE-mediated allergic disorders, anti-IgE therapeutic development, and fundamental studies of humoral immunity. Its validated performance in ELISA makes it particularly suited for quantitative detection of IGHE in serum samples or recombinant protein characterization studies.