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IL4R

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All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Background

Interleukin 4 receptor alpha (IL-4Rα), encoded by the IL4R gene and also known as CD124, is a type I transmembrane cytokine receptor subunit expressed in multiple hematopoietic and non-hematopoietic cell populations, including lymphoid, myeloid, and epithelial cells. Rather than functioning as a complete receptor on its own, IL-4Rα participates in two heteromeric receptor complexes. In the type I IL-4 receptor, IL-4 first binds IL-4Rα and promotes recruitment of the common gamma chain (γc/IL2RG). In the type II receptor, IL-4 similarly binds IL-4Rα before recruitment of IL13Rα1, whereas IL-13 follows the opposite assembly sequence, initially binding IL13Rα1 and subsequently recruiting IL-4Rα. Formation of these receptor complexes activates associated JAK-family kinases and downstream signaling pathways, prominently including STAT6, which contribute to the regulation of type 2 immune responses and related cellular programs. Through its participation in these receptor systems, IL-4Rα is involved in processes such as T-cell differentiation, B-cell responses, macrophage polarization, and epithelial responses to type 2 cytokines, making it an important research target for cytokine receptor assembly, signaling, and type 2 immune biology.

IL-4Rα functions as a shared receptor component that connects IL-4 and IL-13 signaling through distinct heteromeric receptor configurations. IL-4 engagement of IL-4Rα can initiate assembly of either the type I receptor with γc or the type II receptor with IL13Rα1, while IL-13 signaling through the type II receptor begins with binding to IL13Rα1 followed by recruitment of IL-4Rα. These assembled complexes support intracellular JAK-STAT signaling and other context-dependent pathways that regulate gene expression and cellular responses. IL-4Rα therefore contributes to the coordination of type 2 cytokine responses across immune and epithelial cell systems without independently serving as a dual IL-4/IL-13-binding receptor. Its receptor-subunit function makes IL-4Rα a useful target for research on heteromeric cytokine receptor organization, ligand-dependent signaling, immune cell differentiation, and type 2 inflammatory pathway biology.

Fig. 1 Schematic of dual IL4 receptor subtypes and multi-branched JAK-STAT/PI3K/ERK inflammatory signaling pathway. (OA Literature)Fig. 1 Assembly and downstream signaling cascades of type I and type II IL4 receptor complexes in hematopoietic and non-hematopoietic cells upon IL-4 or IL-13 stimulation.1

IL4R Protein Function: Roles in IL-4/IL-13 Receptor Assembly and Type 2 Cytokine Signaling

IL-4Rα, encoded by the IL4R gene, functions as a shared receptor subunit in the type I and type II cytokine receptor complexes involved in IL-4 and IL-13 signaling:

  • IL-4 Recognition and Receptor Assembly: IL-4 initially binds IL-4Rα and promotes recruitment of either the common gamma chain (γc/IL2RG) to form the type I IL-4 receptor or IL13Rα1 to form the type II receptor.
  • IL-13 Receptor Complex Formation: IL-13 first binds IL13Rα1, which subsequently recruits IL-4Rα to assemble the signaling-competent type II receptor complex.
  • JAK-STAT6 Signaling: Formation of the appropriate heteromeric receptor complex activates receptor-associated JAK kinases and downstream STAT6 signaling, contributing to type 2 cytokine-responsive gene expression.
  • Type 2 Immune Regulation: IL-4Rα-containing receptor complexes participate in the regulation of T-cell differentiation, B-cell responses, macrophage polarization, and other immune processes associated with IL-4 and IL-13 signaling.
  • Epithelial and Immune Cell Responses: Through the type II receptor complex, IL-4Rα also contributes to IL-4- and IL-13-responsive signaling in epithelial and other non-hematopoietic cell populations, supporting research into cytokine receptor biology and type 2 inflammatory pathways.

IL4R Protein Product

Creative Biolabs offers high-quality IL4Rα proteins produced using optimized expression systems, including full-length receptor alpha subunit and isolated extracellular domain variants. The IL4Rα extracellular domain directly mediates IL-4 binding, making these proteins suitable for IL-4 receptor-ligand interaction studies and related molecular characterization. In the type II IL-4/IL-13 receptor complex, IL-13 initially binds IL13Rα1, followed by recruitment of IL4Rα; therefore, studies of IL-13 receptor-complex formation or downstream signaling require appropriate systems containing IL13Rα1 and other relevant cellular signaling components. All IL4Rα proteins undergo strict quality control to support consistent performance across applicable research platforms.

IL4R Protein Product

Not finding the membrane protein product you need? Contact us to start your one-stop custom service!

IL4R Stable Cell Line Product

Creative Biolabs provides custom-engineered IL4R stable cell lines, including overexpression and blank control models. These cell lines are optimized for cytokine receptor profiling and Th2 differentiation signal functional analysis. Each cell line undergoes stringent validation to ensure stable expression profiles and consistent functional performance in diverse experimental contexts.

IL4R Stable Cell Line Product

Not finding the stable cell line product you need? Contact us to start your one-stop custom service!

IL4R Recombinant Antibody Product

High-specificity recombinant antibodies targeting IL4R are developed using antibody engineering technologies for research applications involving IL4R expression and localization. These antibodies can be used in studies of IL4R distribution in relevant cell and tissue models and may also support characterization of IL4R-containing receptor complexes in combination with appropriate IL-4, IL-13, or related receptor-component detection reagents.

IL4R Recombinant Antibody Product

Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!

Product Features

  • Native IL-4/IL-13 Ligand Binding Activity: Preserves intact type 2 cytokine recognition capacity for allergic immunity research.
  • IL4R Subunit Specificity: Eliminates non-specific cross-recognition of unrelated interleukin receptor chains.
  • Allergic Immunology Compatibility: Optimized reagent series for Th2 polarization and anti-allergic therapeutic screening workflows.
  • Comprehensive Customization Support: Facilitates end-to-end development of customized proteins, antibodies and stable cell lines to address type 2 cytokine receptor research demands.

Custom IL4R Research Services

Beyond catalog products, Creative Biolabs offers specialized custom services for IL4R research:

  • Custom IL4R Protein Production: Tailored expression of mutant and tagged IL4R constructs for interleukin ligand binding analysis.
  • Custom Antibody Development: Generation of IL4R-specific antibodies for immune membrane immunostaining.
  • Stable Cell Line Engineering: Construction of IL4R-modified cell models for STAT Th2 signaling research.
  • Functional Assay Development: Custom design of cytokine binding and lymphocyte differentiation detection workflows.

Frequently Asked Questions (FAQ)

  1. What is the primary function of IL4R?

    IL4R is a heteromeric type I cytokine receptor binding IL-4/IL-13 to activate STAT signaling and drive Th2 allergic immune differentiation.

  2. Why is IL4R a significant research target?

    IL4R is the central receptor governing type 2 immunity, a core target for allergy and inflammatory disorder study.

  3. Are Creative Biolabs' IL4R products suitable for clinical use?

    No, all IL4R products and services are strictly for research use only, not intended for clinical diagnosis or treatment.

  4. What types of IL4R products does Creative Biolabs offer?

    Offerings include full-length IL4R membrane glycoproteins, isoform-specific detection antibodies and custom stable cell lines for type 2 immunity research.

  5. How are IL4R proteins validated for activity?

    IL4R proteins are validated via IL-4/IL-13 ligand binding functional testing.

Reference
  1. Shi, Jingwei, et al. "Involvement of IL-4, IL-13 and their receptors in pancreatic cancer." International journal of molecular sciences 22.6 (2021): 2998. Under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/ijms22062998
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