Alias: Interleukine-4

Price : 483 Euro / 50µg

IL-4 is a TH2 anti-inflammatory cytokine that is secreted by activated TH2 and NKT cells, and to a lesser extent by TH1 and mast cells. IL-4 exerts numerous effects on various hematopoietic cell types by biding to either type I or Type II IL-4R (the latter of which IL-13 also binds to and as such is also referred to as IL-13R). IL-4, by the means of STAT6 and GATA3, promotes TH2 cell differentiation that produces IL-4, IL-5, and IL-13. In B cells, IL-4 promotes proliferation and differentiation, promotes immunological class switching to IgE and IgG1 isotypes (in conjunction with other signals such as CD40), and upregulates MHC class II and CD23 expression. In T and B lymphocytes, mast cells, and endothelial cells, IL-4 promotes survival, growth, and differentiation. In macrophages, IL-4 can inhibit the production of TNF, IL-1, and IL-6. With its relevance to disease, IL-4 is an immune-stimulating molecule. As such it is one of the more recent targets being studied for new asthma treatments.


Product Description

Interleukin-4 (IL-4) is a pleiotropic cytokine that regulates diverse T and B cell responses including differentiation of naive T cells into the TH2 phenotype, promoting B cell proliferation, antibody isotype switching, and expression of other TH2 cytokines including IL-5 and IL-9.1,2 IL-4plays a critical role in the development of allergic inflammation and asthma.3

IL-4 binds to two distinct receptors; the type I receptor, a heterodimer consisting of the IL-4Rαchain and the common gamma chain, γc, and the type II receptor, a heterodimer of IL-4Rαand IL-13Rα1.4

Naturally occurring IL-4 has a molecular mass of 12–20 kDa. Recombinant human IL-4 is a 14.9 kDa protein containing 129 amino acid residues. Human and mouse IL-4 share a 50% amino acid sequence homology, but their biological actions are speciesspecific.5

This product is lyophilized from a sterile-filtered solution without carrier protein.

Purity: 98% (SDS-PAGE)

ED50: 0.4 ng/mL

The biological activity of human IL-4 is tested in culture using a factor dependent cell line, TF-1.6 The ED50 is defined as the effective concentration of growth factor that elicits a 50% increase in cell growth in a cell based bioassay.

Endotoxin: 1 EU/µg protein

Precautions and Disclaimer

This product is for R&D use only, not for drug, household, or other uses. Please consult the Material Safety Data Sheet for information regarding hazards and safe handling practices. 

Preparation Instructions

Reconstitute the contents of the vial using sterile water to a concentration of 0.1 mg/mL. This solution can be further diluted into other aqueous buffers and stored at 2–8 °C for up to 1 week or at –20 °C for extended use.


Store the lyophilized product at –20 °C.

Reconstituted IL-4 should be stored in working aliquots at –20 °C. Repeated freezing and thawing, or storage in frost-free freezers is not recommended.

Basic info

The interleukin 4 (IL4) is a cytokine that induces differentiation of naive helper T cells (Th0 cells) to Th2 cells. Upon activation by IL-4, Th2 cells subsequently produce additional IL-4 in a positive feedback loop. The cell that initially produces IL-4, thus inducing Th0 differentiation, has not been identified, but recent studies suggest that basophils may be the effector cell. It is closely related and has functions similar to Interleukin 13.

It has many biological roles, including the stimulation of activated B-cell and T-cell proliferation, and the differentiation of B cells into plasma cells. It is a key regulator in humoral and adaptive immunity. IL-4 induces B-cell class switching to IgE, and up-regulates MHC class II production. IL-4 decreases the production of Th1 cells, macrophages, IFN-gamma, and dendritic cell IL-12.
Overproduction of IL-4 is associated with allergies.

Inflammation and wound repair
Tissue macrophages play an important role in chronic inflammation and wound repair. The presence of IL-4 in extravascular tissues promotes alternative activation of macrophages into M2 cells and inhibits classical activation of macrophages into M1 cells. An increase in repair macrophages (M2) is coupled with secretion of IL-10 and TGF-β that result in a diminution of pathological inflammation. Release of arginase, proline, polyaminases and TGF-β by the activated M2 cell is tied with wound repair and fibrosis.

The receptor for Interleukin-4 is known as the IL-4Rα. This receptor exists in 3 different complexes throughout the body. Type 1 receptors are composed of the IL-4Rα subunit with a common γ chain and specifically bind IL-4. Type 2 receptors consist of an IL-4Rα subunit bound to either another IL-4Rα, or a different subunit known as IL-13Rα1. These type 2 receptors have the ability to bind both IL-4 and IL-13, two cytokines with closely related biological functions.

IL-4 has a compact, globular fold (similar to other cytokines), stabilised by 3 disulphide bonds. One half of the structure is dominated by a 4 alpha-helix bundle with a left-handed twist. The helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet.

This cytokine was co-discovered by Maureen Howard and William Paul and by Dr. Ellen Vitetta and her research group in 1982.
The nucleotide sequence for human IL-4 was isolated four years later confirming its similarity to a mouse protein called B-cell stimulatory factor-1 (BCSF-1).


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

2.     O’Garra, A., and Arai, N., The molecular basis of T helper 1 and T helper 2 cell differentiation. Trends Cell Biol., 10, 542-550 (2000).

3.     Ryan, J.J. et al., Mast cell homeostasis: a fundamental aspect of allergic disease. Crit. Rev. Immunol., 27, 15-32 (2007).

4.     Callard, R.E. et al., IL-4 and IL-13 receptors: are they one and the same? Immunol. Today, 17, 108110 (1996).

5.     Yokota, T. et al., Molecular biology of interleukin 4 and interleukin 5 genes and biology of their products that stimulate B cells, T cells and hemopoietic cells. Immunol. Rev., 102, 137-187 (1988).

6.     Kitamura, T. et al., Establishment and characterization of a unique human cell line that proliferates dependently on GM-CSF, IL-3, or erythropoietin. J. Cell Physiol., 140, 323-334 (1989).