Fc epsilon RIα (FcεRIα), also known as the high-affinity IgE receptor alpha chain, is the IgE-binding subunit of the high-affinity FcεRI receptor complex. It is primarily expressed on mast cells and basophils, where it mediates IgE-dependent allergic responses, and can also be detected on additional immune cell populations involved in antigen presentation and regulation of IgE responses. Binding of IgE to FcεRIα plays a central role in allergen-induced cell activation and mediator release. FcεRIα is widely studied in allergic inflammation, asthma, atopic diseases, and mast cell biology. In addition to its role on effector cells, soluble and recombinant forms of FcεRIα have been shown to interact with membrane-bound IgE on IgE-bearing B cells and modulate IgE synthesis, highlighting the importance of FcεRIα in both allergic effector mechanisms and regulation of IgE responses.
Clone AER-37 [CRA1] is a mouse monoclonal antibody recognizing an extracellular epitope of human FcεRIα. Originally described together with clone CRA2 in studies characterizing recombinant soluble FcεRIα, CRA1 was shown to bind FcεRIα without competing with IgE for receptor binding. This property makes the antibody particularly useful for detection of FcεRIα independently of IgE occupancy. Clone AER-37 [CRA1] recognizes an extracellular epitope of Fc epsilon RIα and is well suited for flow cytometry, immunocytochemistry, immunohistochemistry, and Western blot applications. The antibody enables reliable identification and characterization of FcεRIα-expressing cell populations, particularly basophils and mast cells, through strong and specific surface staining. The following images show the results of the functionality verification using flow cytometry (descriptions for the individual images will be displayed after opening them).
Would you like to have our antibodies in other formats? Let us know by e-mail or use our FORM! Contact: info@exbio.cz