Recombinant Human IL-4 (carrier-free)

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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.
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Cat # Size Price Quantity Avail. Save
574008 500 µg 1 800 CHF
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574002 10 µg 125 CHF
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574004 25 µg 215 CHF
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574006 100 µg 650 CHF
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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 (please contact technical support for concentration, or use our Lookup tool if you have a lot number.)

Please note, new lots of the 100 µg size will be lot-specific and may differ from previous lots that had a fixed concentration.
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

(PubMed link indicates BioLegend citation)
  1. Chalubinski M, et al. 2014. Food Chem Toxicol. 69:289. PubMed
Product Citations
  1. Yamada KJ, et al. 2020. PLoS Pathog. 16:e1008354. PubMed
  2. Brasil da Costa FH, et al. 2020. PLoS One. 15:e0230354. PubMed
  3. Zhang H, et al. 2020. Front Cell Dev Biol. 8:205. PubMed
  4. Wang LW, et al. 2019. Cell Metab. 30:539. PubMed
  5. Guo J, et al. 2019. Cancer Immunol Res. 1.349305556. PubMed
  6. Chalubinski M, et al. 2014. Food Chem Toxicol. 69:289. PubMed
  7. Wu W, et al. 2015. Am J Pathol. 185: 2324-2335. PubMed
  8. Koh WH, et al. 2020. STAR Protoc. 1:100203. PubMed
  9. Trapecar M, et al. 2021. Sci Adv. 7:00. 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) = 10e6/ ED50 (ng/mL)
Go To Top Version: 5    Revision Date: 06.11.2021

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

BioLegend Inc., 8999 BioLegend Way, San Diego, CA 92121 www.biolegend.com
Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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