Recombinant Mouse IL-4 (Animal-Free)

Pricing & Availability
Regulatory Status
Other Names
Interleukin-4, B-cell stimulating factor-1 (BSF-1), Ia inducing factor (IaIF), Hodgkin's cell growth factor (HCGF), Mast cell growth factor-2 (MCGF-2), Macrophage fusion factor (MFF), T cell growth factor-2 (TCGF-2)
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Product Citations
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715004 20 µg 203€
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IL-4 is a member of the short four-helix bundle family of cytokines. IL-4 is produced by Th2 cells in response to antigen receptor engagement. Dendritic cells can prime naïve CD4+ T cell; nevertheless, it has been described that dendritic cell mediated priming is insufficient for the development of Th2 cell-dependent immunity. Basophils have been identified as a source of IL-4 in the initial naïve CD4+ T cell priming. These cells coexpress MHC class II and IL-4 following helminth infection. Therefore, murine basophils could present antigens to naïve T cells, thus promoting Th2 cell differentiation during allergic and anti-parasitic immune responses. In addition, it was previously known that upon cross-linkage of the high affinity receptor for immunoglobulin E, IL-4 is produced by NK cells, mast cells, and basophils. Cells of hematopoietic stem cell origin express the type I receptor for IL-4 (IL-4Ra, γc), and cells of non-hematopoietic stem cell origin express type II receptor (IL-4Ra, IL-13Ra1). Type I receptor complexes are active in regulating Th2 development. In contrast, the type II receptor complex is active in regulating cells that mediate airway hypersensitivity and mucus secretion.

Product Details
Technical Data Sheet (pdf)

Product Details

Mouse IL-4, amino acids His21-Ser140 (Accession# NM_021283), was expressed in E. coli.
Molecular Mass
The 121 amino acid N-terminal methionylated recombinant protein has a predicted molecular mass of 13.5 kD. The predicted N-terminal amino acid is Met.
>98%, as determined by Coomassie stained SDS-PAGE and HPLC analysis.
Lyophilized, carrier-free.
Endotoxin Level
Less than 0.1 ng per µg of protein.
Storage & Handling
Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. It is recommended to further dilute in a buffer, such as 5% Trehalose, and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
ED50 is ≤ 2.0 ng/ml, corresponding to a specific activity of ≥ 5.0 x 105 units/mg as determined by the dose-dependent stimulation of the proliferation of murine HT-2 cells.


Product Citations
  1. Boothby IC, et al. 2021. Nature. 599:667. PubMed
  2. He X, et al. 2020. J Immunother Cancer. 8:00. PubMed
  3. Patel J, et al. 2022. Int J Biol Sci. 18:2670. PubMed
  4. Hodgson R, et al. 2022. Commun Biol. 5:1216. PubMed

Antigen Details

IL-4 is produced by Th2 cells, NK T cells, mast cells, basophils, eosinophils, and macrophages.
IL-4 plays a crucial role in the differentiation of Th2 cells and induction of Th2 associated cytokines. IL-4, through its activation of STAT6, upregulates GATA3 expression and also suppresses Th1 and Th17 cell responses, partly through the upregulation of growth factor independent 1 (GFI1), a transcriptional repressor of IFNγ and IL-17 production. IL-4 induces macrophage activation and TSLP production. IL-4 recruits and activates IgE-producing B cells (IgE class switching) and enhances IgE-mediated responses by up-regulating IgE receptors on B lymphocytes, mast cells, and basophils. In addition, IL-4 also induces VCAM-1 on vascular endothelium and thus directs the migration of T lymphocytes, monocytes, basophils, and eosinophils to the inflammation site.
T cells, B cells, mast cells, monocytes, macrophages, fibroblast, and endothelial cells.
IL-4 signals through type I (IL-4Rα, γc) and type II receptor (IL-4Rγ, IL-13Rα1) complexes.
Cell Type
Hematopoietic stem and progenitors, Embryonic Stem Cells
Biology Area
Cell Biology, Stem Cells, Immunology
Molecular Family
Antigen References

1. Chen. L, et al. 2004. J. Immunol. 172:2059.
2. Maroof A, et al. 2006. Immunology 117:271.
3. Sharma P, et al. 2008. Immunity 29:551.
4. Heller NM, et al. 2008. Sci. Signal 1:ra17.
5. LaPorte SL, et al. 2008. Cell 132:259.
6. Perrigoue JG, et al. 2009. Nat. Immunol. 10:697.
7. Schneider E, et al. 2010. Eur. Cytokine Netw. 21:142.
8. Leavy O. 2011. Nat. Rev. Immunol. doi:10.1038/nri2908.

Gene ID
16189 View all products for this Gene ID
View information about IL-4 on

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 3    Revision Date: 05/06/2014

For Research Use Only. Not for diagnostic or therapeutic use.


This product is supplied subject to the terms and conditions, including the limited license, located at ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.


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