Recombinant human IL-4 protein (Qk092)

Interleukin-4 (IL-4) is a pleiotropic, immune-modulatory cytokine that is secreted primarily by mast cells, T-cells, eosinophils, and basophils. IL-4 plays a crucial role in hematopoiesis, the regulation of antibody production, the stimulation of activated B cell and T cell proliferation, and the differentiation of B cells into plasma cells

Human IL-4 has a molecular weight of 15.1 kDa. This protein is animal origin-free, carrier-free and tag-free to ensure its purity with exceptional lot-to-lot consistency. Qk092 is suitable for the culture of reproducible and high-quality stem cells and other relevant cells.

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1000µg will be despatched as 2 x 500µg

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Summary

  • High purity human protein (Uniprot number: P05112)

  • >98%, by SDS-PAGE quantitative densitometry

  • Source: Expressed in E. coli 

  • 15.1 kDa monomer

  • Animal origin-free (AOF) and carrier protein-free

  • Manufactured in Cambridge, UK

  • Lyophilized from acetonitrile/TFA

  • Resuspend in water at >100 µg/mL, prepare single-use aliquots, add carrier protein if desired, and store frozen at -20oC or -80oC

Featured applications

  • Stimulation of activated B cell proliferation

  • Stimulation of activated T cell proliferation

  • Differentiation of B cells into plasma cells

  • Adaptive immunity regulator
  • Antibody regulation
  • Lymphoid differentiation

Interleukin-4
B-cell stimulatory factor 1 (BSF-1)
Binetrakin
Lymphocyte stimulatory factor 1
Pitrakinra

Bioactivity

Bioactivity graph showing the EC50 of 235 pg/ml (16 pM) for Qkine recombinant IL-4

IL-4 activity is determined using proliferation of TF-1 human myeloid leukemia cells. EC50 = 235 pg/mL (16 pM). Cells are treated in triplicate with a serial dilution of IL-4 for 72 hours. Cell viability is measured using the CellTiter-Glo (Promega) luminescence assay. Data from Qk092 lot #204598. 

Purity

SDS PAGE: SDS-PAGE gel showing the high purity reduced and non-reduced forms of IL-4

Recombinant IL-4 migrates as a major band at approximately 14 kDa in non-reducing (NR) and at approximately 12.5 kDa in reduced (R) conditions. No contaminating protein bands are present. The purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced conditions and stained with Coomassie Brilliant Blue R250. Data from Qk092 batch #204598. 

Further quality assays

  • Mass spectrometry, single species with the expected mass

  • Endotoxin: <0.005 EU/μg protein (below the level of detection)

  • Recovery from stock vial: >95%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Qkine IL-4 is as biologically active as a comparable alternative supplier protein

Stimulation of proliferation of TF-1 cells with Qkine IL-4 (Qk092, green) and alternative supplier IL-4 (Supplier B, black). Cells were treated in triplicate with a serial dilution of IL-4 for 72 hours and proliferation measured using the CellTiter-Glo (Promega) luminescence assay.

Protein background

Interleukin 4 (IL-4) is an important signaling molecule within the immune system, playing multiple roles in orchestrating immune responses and maintaining immune homeostasis. IL-4 is primarily produced by immune cells, including mast cells, T helper 2 (Th2) cells, eosinophils, and basophils, and exerts its effects through interaction with its specific receptor, IL-4Rα and subsequent activation of downstream signaling pathways [1]. IL-4 plays a crucial role in hematopoiesis, the regulation of antibody production, the stimulation of activated B cell and T cell proliferation, and the differentiation of B cells into plasma cells. IL-4 induces the expression of class II MHC molecules on resting B-cells and aids regulation of the low-affinity Fc receptor for IgE (CD23) expression on lymphocytes and monocytes [2].

IL-4 has a compact, globular fold stabilized by three disulfide bonds. IL-4 consists of a characteristic four-alpha helix bundle with a left-handed twist, along with a two-stranded anti-parallel beta-sheet [2-3]. This structural arrangement allows stability to IL-4 and also facilitates its interaction with its receptor, IL-4Rα. The receptor for IL-4, IL-4Rα, exists in three distinct complexes within the body, each playing a crucial role in mediating IL-4 signaling [4]. Type 1 receptors consist of the IL-4Rα subunit coupled with a common gamma chain, while type 2 receptors comprise the IL-4Rα subunit bound to IL-13Rα1. Type 1 receptors specifically bind IL-4, whereas type 2 receptors have the capacity to bind both IL-4 and IL-13, two cytokines with closely related functions. This differential receptor composition allows for nuanced regulation of immune responses depending on the specific ligands present [5].

IL-4 serves as a regulator of immune cell differentiation and activation. It promotes the differentiation of naive T cells into Th2 cells, which are crucial for orchestrating immune responses against extracellular pathogens and for mediating allergic reactions. Additionally, IL-4 stimulates the proliferation and activation of B cells, leading to the production of antibodies and the formation of memory B cells [8]. IL-4 plays a pivotal role in modulating macrophage polarization and the development of an alternative activation phenotype (M2) associated with tissue repair and resolution of inflammation [9].

In the context of disease, dysregulation of IL-4 signaling has been implicated in various immune disorders, including allergies, asthma, and autoimmune diseases. Enhanced IL-4 production or aberrant IL-4 receptor signaling can contribute to the pathogenesis of allergic inflammation and tissue damage. Therapeutic strategies aimed at targeting IL-4 or its receptor have shown promise in treating these conditions by modulating immune responses and dampening inflammation [8-10].

[1] Paul, W. E. Interleukin 4: a prototypic immunoregulatory lymphokine. Blood 77, 1859–1870 (1991).

[2] Gadani, S. P., Cronk, J. C., Norris, G. T., & Kipnis, J. IL-4 in the brain: a cytokine to remember. Journal of Immunology 189, 4213–4219 (2012).

[3] Nelms, K., Keegan, A. D., Zamorano, J., Ryan, J. J., & Paul, W. E. The IL-4 receptor: signaling mechanisms and biologic functions. Annual Review of Immunology 17, 701–738 (1999).

[4] Nelms, K., Keegan, A. D., Zamorano, J., Ryan, J. J., & Paul, W. E. The IL-4 receptor: signaling mechanisms and biologic functions. Annual Review of Immunology 17, 701–738 (1999).

[5] Finkelman, F. D., & Urban Jr, J. F. The other side of the coin: the protective role of the TH2 cytokines. Journal of Allergy and Clinical Immunology 102, 705–706 (1998).

[6] Ul-Haq, Z., Naz, S., & Mesaik, M. A. Interleukin-4 receptor signaling and its binding mechanism: A therapeutic insight from inhibitors tool box. Cytokine & Growth Factor Reviews 32, 3–15 (2016).

[7] Gordon, S., & Martinez, F. O. Alternative activation of macrophages: mechanism and functions. Immunity 32, 593–604 (2010).

[8] Chatila, T. A. Interleukin-4 receptor signaling pathways in asthma pathogenesis. Trends in Molecular Medicine 10, 493–499 (2004).

[9] Bhattarai, P. et al. IL4/STAT6 Signaling Activates Neural Stem Cell Proliferation and Neurogenesis upon Amyloid-β42 Aggregation in Adult Zebrafish Brain. Cell Reports 17, 941–948 (2016).

[10] Hershey, G. K. IL-13 receptors and signaling pathways: an evolving web. Journal of Allergy and Clinical Immunology 111, 677–690 (2003).

Additional resources

Our products are for research use only and not for diagnostic or therapeutic use.  Products are not for resale.

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