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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

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. IL-4 additionally is a key regulator in adaptive immunity.

Human IL-4 has a molecular weight of 15.1 kDa. This protein is 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.

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1mg will be despatched as 2 x 500µg

Buy online with secure credit card or purchase order or email orders@qkine.com
Bulk and stock reservation available

Summary

  • High purity human protein (Uniprot number: P05112)

  • >98%, by SDS-PAGE quantitative densitometry

  • Source: Expressed in E. coli 

  • 15.1 kDa monomer

  • Animal-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

  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).

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.

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].

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

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