FCER1A Human
Description
Product Specs
Product Science Overview
Fc-Epsilon RI-Alpha (FcεRIα) is a high-affinity receptor for the Fc region of immunoglobulin E (IgE), an antibody isotype involved in allergic reactions and immunity against parasites . This receptor plays a crucial role in the allergic response by binding to IgE and triggering the release of inflammatory mediators from mast cells and basophils .
FcεRI is a tetrameric receptor complex composed of one alpha (α) chain, one beta (β) chain, and two gamma (γ) chains . The alpha chain (FcεRIα) is responsible for binding to the Fc region of IgE . This binding is essential for the receptor’s role in mediating allergic responses. When an allergen cross-links IgE bound to FcεRIα on the surface of mast cells or basophils, it triggers a cascade of signaling events leading to the release of histamine and other inflammatory mediators .
Recombinant FcεRIα is typically produced using mammalian cell expression systems, such as Chinese Hamster Ovary (CHO) cells or mouse myeloma cells . These systems are chosen for their ability to perform post-translational modifications, which are crucial for the proper folding and function of the protein. The recombinant protein is often tagged with a His-tag or Avi-tag to facilitate purification and detection .
The production of recombinant FcεRIα involves several key steps:
- Gene Cloning: The gene encoding FcεRIα is cloned into an expression vector suitable for the chosen mammalian cell system.
- Transfection: The expression vector is introduced into the mammalian cells using methods such as electroporation or lipid-mediated transfection.
- Selection and Expansion: Transfected cells are selected using antibiotic resistance markers and expanded in culture to produce large quantities of the recombinant protein.
- Purification: The recombinant protein is purified from the culture supernatant using affinity chromatography techniques, such as nickel affinity chromatography for His-tagged proteins .
FcεRIα’s interaction with IgE is a critical aspect of its function. The binding affinity between FcεRIα and IgE is extremely high, which ensures that even low concentrations of IgE can trigger an allergic response . This high-affinity binding is mediated by specific interactions between the Fc region of IgE and the extracellular domain of FcεRIα . The cross-linking of IgE-FcεRIα complexes by allergens leads to the activation of intracellular signaling pathways, resulting in the release of histamine and other mediators .
