Recombinant Human IL-4 (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
B cell growth factor 1 (BCGF-1), B-cell stimulatory factor 1 (BSF-1), interleukin-4, lymphocyte stimulatory factor 1, MGC79402
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Product Citations
publications
Human_IL-4_carrfree_070110
Human IL-4 induces proliferation of TF‑1 human erythroleukemic cells.
  • Human_IL-4_carrfree_070110
    Human IL-4 induces proliferation of TF‑1 human erythroleukemic cells.
  • Recombinant_Human_IL-4_CF_012022
    Recombinant human IL-4 induces the proliferation of TF-1 human erythroleukemic cells in a dose dependent manner. BioLegend’s protein was compared side-by-side to a competitor’s equivalent product.
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574008 500 µg 1688€
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574002 10 µg 118€
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574004 25 µg 203€
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574006 100 µg 610€
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Description

IL-4 is the primary cytokine implicated in the development of Th2-mediated responses, which is associated with allergy and asthma. The Type I receptor comprises IL-4Rα and the common gamma-chain (γc), which is also shared by the cytokines IL-2, -7, -9, -15 and -21 and is present in hematopoietic cells. IL-4 can use the type II complex, comprising IL-4Rα and IL-13Rα1, which is present in non-hematopoietic cells. This second receptor complex is a functional receptor for IL-13, which shares approximately 25% homology with IL-4. The type I receptor complex can be formed only by IL-4 and is active in Th2 development. In contrast, the type II receptor complex formed by either IL-4 or IL-13 is more active during airway hypersensitivity and mucus secretion and is not found in T cells.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Human IL-4, amino acids His25-Ser153 (Accession# NM_000589) was expressed in E.coli.
Molecular Mass
The 130 amino acid recombinant protein has a predicted molecular mass of approximately 15.1 kD. The N-terminal amino acid is Met.
Purity
Purity is >95%, as determined by Coomassie stained SDS-PAGE.
Formulation
The protein was 0.22 µm filtered in PBS, pH 7.2.
Endotoxin Level
Less than 0.01ng per µg cytokine as determined by the LAL method
Preparation
For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 µg/mL in sterile buffer containing carrier protein such as 1% BSA or HSA or 10% FBS.
Concentration
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
ED50 = 0.04 - 0.2 ng/mL as determined by the dose-dependent stimulation of TF-1 cell proliferation.

The specific activity of recombinant human IL-4 is approximately 1.02 x 104 IU/µg when compared against the 1st WHO International Standard for Human Interleukin-4 (NIBSC code: 88/656) as determined by the dose-dependent stimulation of TF-1 cell proliferation.

For more information on specific activity, please visit the Recombinant Protein Unit Conversions page.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Application References
  1. Chalubinski M, et al. 2014. Food Chem Toxicol. 69:289. PubMed
Product Citations
  1. Duhen R, et al. 2022. J Clin Invest. 132: . PubMed
  2. Chen WLK, et al. 2021. ACS Infect Dis. 7:838. PubMed
  3. Zhang J, et al. 2023. Cell Death Dis. 737:14. PubMed
  4. Zhang C, et al. 2021. Proc Natl Acad Sci U S A. 118:. PubMed
  5. Coray M, et al. 2022. Int J Mol Sci. 23:. PubMed
  6. Zhang H, et al. 2020. Front Cell Dev Biol. 8:205. PubMed
  7. Moran MC, et al. 2022. JID Innov. :100151. PubMed
  8. Baleeiro RB, et al. 2022. Oncoimmunology. 11:2080329. PubMed
  9. Guo J, et al. 2019. Cancer Immunol Res. 1.349305556. PubMed
  10. Trapecar M, et al. 2021. Sci Adv. 7:00. PubMed
  11. Fosdick MG, et al. 2022. Sci Rep. 12:13506. PubMed
  12. Wu W, et al. 2015. Am J Pathol. 185: 2324-2335. PubMed
  13. Yamada KJ, et al. 2020. PLoS Pathog. 16:e1008354. PubMed
  14. Yamaguchi Y, et al. 2022. J Immunother Cancer. 10:. PubMed
  15. Wang LW, et al. 2019. Cell Metab. 30:539. PubMed
  16. Brasil da Costa FH, et al. 2020. PLoS One. 15:e0230354. PubMed
  17. Chalubinski M, et al. 2020. APMIS. 128:10. PubMed
  18. Arora S, et al. 2021. Med (N Y). 2:938. PubMed
  19. Koh WH, et al. 2020. STAR Protoc. 1:100203. PubMed
  20. Chalubinski M, et al. 2014. Food Chem Toxicol. 69:289. PubMed

Antigen Details

Structure
Heterodimer
Distribution

IL-4 is produced by Th2 cells, naive CD4+ T cells, NKT cells, and basophils.

Function
IL-4 has 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.
Interaction
T cells, B cells, macrophages, epithelial cells, smooth muscle cells, and bronchial fibroblasts.
Ligand/Receptor
IL-4 signals through Type I (IL-4Rα, γc) and Type II receptors (IL-4Rα, IL-13Rα1) complexes.
Cell Type
Embryonic Stem Cells, Hematopoietic stem and progenitors
Biology Area
Cell Biology, Immunology, Stem Cells
Molecular Family
Cytokines/Chemokines
Antigen References

1. Swain SL, et al. 1990. J. Immunol. 145:3796.
2. Hsieh CS, et al. 1992. P. Natl. Acad. Sci. USA 89:6065.
3. Allison-Lynn A, et al. 2006. J. Immunol. 176:7456.
4. Kato A, et al. 2007. J. Immunol. 179:1080.
5. LaPorte SL, et al. 2008. Cell 132:259.
6. Martinez FO, et al. 2009. Annu. Rev. Immunol. 27:451.

Gene ID
3565 View all products for this Gene ID
UniProt
View information about IL-4 on UniProt.org

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: 5    Revision Date: 06.11.2021

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 www.biolegend.com/terms) ("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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