Mouse interleukin 4 receptor alpha (IL-4Rα) is a Type I transmembrane and a Type 1 cytokine receptor. The recombinant IL-4Rα dimer protein (CSP-25220-01) is a cis-homodimer (cis-dimer) and contains an IL-4Rα extracellular domain (UniProt# P16382, amino acids Ile26-Arg233) fused with a proprietary cis-dimer motif followed by a His tag at the C-terminus. This dimeric protein is expressed in HEK293T cells. The recombinant mouse IL-4Rα dimer protein is bioactive and binds IL-4Rα-specific antibodies. This IL-4Rα dimer can be used as an antigen for in vitro assays and antibody screening, and as an immunogen for immunization to generate antibodies targeting more conformational epitopes.
Protein Name: IL-4Rα
UniProt #: AA: P16382
Predicted Molecular Weight: 65 kDa
SDS PAGE Molecular Weight: The migration range of the heterodimer protein with glycosylation under non-reducing condition is between 120 and 190 kDa on SDS PAGE.
Protein Construct: IL-4Rα dimer protein contains an IL-4Rα extracellular domainfused with a proprietary cis-dimer motif followed by a His tag at the C-terminus.
Background
Interleukin 4 receptor alpha (IL-4Rα) is a Type I transmembrane and a Type 1 cytokine receptor. IL-4Rα is also known as cluster of differentiation 124 (CD124). IL-4Rα is a key component in interleukin 4 (IL-4) and IL-13 cytokine signaling involved in immune regulation, particularly in Th2 immune responses, allergy, and asthma. IL-4Rα contains an extracellular domain with an overall L shape organized in two covalently linked domains: an h-type immunoglobulin fold (D1) and a standard fibronectin type III (FN III)–like topology (D2). IL-4Rα can bind IL-4 and IL-13 and allergic inflammation is largely driven by IL-4 and IL-13 signaling through IL-4Rα, making IL-4Rα a promising therapeutic target for allergic diseases. While structurally and functionally similar to human IL-4Rα homodimer, mouse IL-4Rα homodimer is a species-specific tool essential for preclinical studies, basic research, and translational research.