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Interleukin 2 receptor subunit alpha (IL2RA, also named CD25) is a type I transmembrane glycoprotein encoded by IL2RA gene, selectively upregulated upon T cell activation and constitutively highly expressed on regulatory T cell (Treg) populations, functioning as the ligand capture subunit required to assemble high-affinity trimeric IL-2 receptor complexes together with constitutive IL2RB and IL2RG signaling subunits. The isolated IL2RA subunit lacks cytoplasmic tyrosine kinase motifs and cannot transmit intracellular signals independently; its large heavily glycosylated extracellular domain exclusively binds circulating IL-2 cytokine with moderate standalone affinity, drastically increasing overall receptor ligand avidity when assembled into trimeric receptor assemblies to enable sensitive detection of low physiological IL-2 concentrations within lymphoid tissues. Under steady-state immune tolerance conditions, constitutive IL2RA expression on Tregs creates high-affinity IL-2 sinks that sequester local IL-2 to limit effector T cell proliferative expansion and sustain peripheral immune self-tolerance against self-antigens. Upon acute immune activation, conventional T cells transiently induce IL2RA expression to boost IL-2 responsiveness and support clonal expansion against foreign pathogens. Distinct from permanently expressed IL2RB/IL2RG signaling chains, IL2RA acts as an inducible regulatory subunit that dictates receptor ligand sensitivity threshold, with its expression status serving as a definitive surface biomarker distinguishing functional Treg populations from resting conventional T cells. Genetic IL2RA deficiency abolishes high-affinity IL-2 signal reception, impairs Treg suppressive capacity and triggers severe systemic autoimmune lymphoproliferative disease, while abnormal sustained IL2RA expression amplifies Treg-mediated immune suppression to weaken anti-tumor and anti-pathogen immune defense, establishing IL2RA as a core research target for T cell receptor biology and autoimmune/tumor immunology exploration.
IL2RA executes core ligand capture regulatory function via glycosylated extracellular Ig-like domains that form high-affinity IL-2 binding pockets only stable within trimeric IL2RA-IL2RB-IL2RG membrane receptor assemblies. Without IL2RA incorporation, dimeric IL2RB/IL2RG receptors display low IL-2 affinity and fail to respond to physiological low cytokine concentrations present in resting lymphoid microenvironments. Conserved extracellular carbohydrate modifications stabilize IL-2 ligand binding and protect the receptor from rapid proteolytic shedding at cell surface membranes. IL2RA-dependent high-affinity receptor formation sustains balanced systemic T lymphocyte homeostasis, covering Treg-mediated self-tolerance and controlled effector T cell clonal expansion during infection. IL2RA participates in a broad spectrum of adaptive immune processes including thymic Treg maturation, peripheral immune tolerance maintenance and antigen-driven effector T cell proliferation. Dysregulated IL2RA expression disrupts IL-2 cytokine balance and shifts immune output toward either autoimmune inflammation or excessive tumor immune suppression. Therefore, IL2RA represents a pivotal research target for cytokine receptor subunit study and immune tolerance modulator screening.
Fig. 1 IL2RA enhancer variants tune CD25-mediated IL-2-STAT5 signaling, altering T cell immunity.1
The biological functions of IL2RA are focused on inducible IL-2 ligand sequestration, trimeric receptor assembly and regulatory T cell suppressive tuning:
Creative Biolabs offers high-quality IL2RA proteins through optimized expression systems, including full-length glycosylated membrane subunit and isolated extracellular IL-2 binding domain variants. These products retain native conformational characteristics and IL-2 ligand binding biological activity, suitable for cytokine receptor trimer assembly interaction assays and immune tolerance regulatory compound screening. All IL2RA proteins undergo strict quality control to ensure consistent performance and reliable application across diverse research platforms.
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Creative Biolabs provides custom-engineered IL2RA stable cell lines, including constitutive overexpression and blank control models. These cell lines are optimized for high-affinity IL-2 receptor assembly profiling and Treg suppressive functional analysis. Each cell line undergoes stringent validation to ensure stable expression profiles and consistent functional performance in diverse experimental contexts.
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High-specificity recombinant antibodies targeting IL2RA are developed via advanced antibody engineering technologies, with no cross-reactivity with IL2RB and IL2RG receptor subunits. These antibodies are validated for Treg and activated T cell surface localization detection and lymphoid tissue immune cell subset profiling, and can be combined with IL-2 detection reagents to quantify complete high-affinity trimeric receptor-ligand complexes in tolerance and tumor immune research models.
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Beyond catalog products, Creative Biolabs offers specialized custom services for IL2RA research:
IL2RA/CD25 is the ligand-binding alpha subunit of the high-affinity IL-2 receptor, highly expressed on Tregs to capture IL-2 and maintain peripheral immune self-tolerance.
IL2RA serves as a definitive Treg biomarker and controls IL-2 dependent immune balance, central to autoimmune disease and anti-tumor immunology research.
No, all IL2RA products and services are strictly for research use only, not intended for clinical diagnosis or treatment.
Offerings include glycosylated IL2RA membrane subunit proteins, subset-specific detection antibodies and custom stable cell lines for T cell immune tolerance research.
IL2RA proteins are validated via IL-2 cytokine ligand binding and trimeric receptor assembly interaction testing.