FCER1A Human 201 a.a

The high-affinity immunoglobulin E (IgE) receptor, known as FcεRI, plays a pivotal role in allergic reactions and related disorders. This receptor is primarily expressed on the surface of mast cells and basophils, and it is composed of three subunits: α (alpha), β (beta), and γ (gamma). The α subunit (FcεRIα) is crucial for binding IgE with high affinity, which is essential for initiating the allergic response.

The FcεRI receptor is a heterotetramer consisting of one α subunit, one β subunit, and two γ subunits (αβγ2). The α subunit is responsible for the high-affinity binding of IgE. This binding is a critical step in the allergic response, as it leads to the activation of mast cells and basophils, resulting in the release of histamines and other inflammatory mediators .

Interestingly, the α subunit alone is sufficient for high-affinity IgE binding, even in the absence of the β and γ subunits . This highlights the importance of the α subunit in the receptor’s function.

The gene encoding the α subunit of FcεRI is known as FCER1A. Recent studies have shown significant genetic variability in the FCER1A gene, which can influence the receptor’s function and its role in allergic diseases . Variants in the FCER1A gene have been associated with different levels of serum IgE and susceptibility to allergic disorders .

Recombinant human FcεRIα is produced using various expression systems, such as bacterial, yeast, and mammalian cells. The recombinant protein is used in research to study the receptor’s structure, function, and its role in allergic reactions. It is also used in the development of therapeutic interventions targeting the IgE-FcεRI interaction .

Recombinant FcεRIα is a valuable tool in allergy research. It allows scientists to study the receptor’s binding properties and its interaction with IgE in detail. This knowledge is crucial for developing new therapies for allergic diseases, such as monoclonal antibodies that can block the IgE-FcεRI interaction and prevent allergic reactions .