Recombinant Human IL-2 (carrier-free)

Pricing & Availability
Other Names
T-cell growth factor (TCGF), Eosinophil differentiation factor (EDF), Killer cell helper factor (KHF), Macrophage-activating factor for cytotoxicity I (MAF-C I), Thymocyte differentiation factor (TDF)
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Product Citations
publications
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Recombinant Human IL-2 induces the proliferation of mouse HT-2 cells in a dose-dependent manner. The ED50 for this effect is 0.2 – 1.0 ng/mL.
  • Human_IL-2_CF_RECOM_1_043019.png
    Recombinant Human IL-2 induces the proliferation of mouse HT-2 cells in a dose-dependent manner. The ED50 for this effect is 0.2 – 1.0 ng/mL.
Cat # Size Price Quantity Avail. Save
589102 10 µg $125
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589104 25 µg $225
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589106 100 µg $595
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589108 500 µg $1,900
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Description

IL-2 was discovered through its function as a T cell growth factor (TCGF), and plays a pivotal role in immune responses against pathogenic infection. Recognition and binding of the foreign Ags by the TCRs stimulate both the secretion of IL-2 and the expression of IL-2Rs on the T cell surface. Subsequently, the IL-2/IL-2R interaction activates the intracellular Ras/Raf/MAPK, JAK/STAT, and PI3K/AKT signal pathways, and ultimately stimulates the growth, differentiation, and survival of the Ag-selected cytotoxic T cells. Human IL-2 acts on murine and human T cells, and its receptors are shared by others cytokines. IL-2Rα is an IL-2–specific receptor, IL-2Rβ is shared with IL-15 and the γ chain that is a common receptor shared by many cytokines including IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21.

Product Details
Technical data sheet

Product Details

Reactivity
Human
Source
Human IL-2, amino acids Ala21-Thr153 (Accession # NM_000586), was expressed in insect cells.
Molecular Mass
The 133 amino acid recombinant protein (Ala21-Thr153) has a predicted molecular mass of 15418 Da. The DTT-reduced and the non-reduced protein migrate at approximately 15 kD by SDS-PAGE. The N-terminal amino acid is Ala.
Purity
Purity is >95%, as determined by Coomassie stained SDS-PAGE.
Formulation
The protein was 0.22 µm filtered protein solution is in 10mM NaH2PO4, pH 7.2, 150mM NaCl.
Endotoxin Level
Less than 0.01 ng per µg cytokine as determined by the LAL method.
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 one month, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored from -20°C to -70°C. Stock solutions can also be prepared at 50-100 µg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2-1% BSA or HSA and stored in working aliquots at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Activity
The ED50 = 0.05 – 0.3 ng/mL as determined by the dose-dependent stimulation of CTLL2 cell proliferation. The ED50 = 0.2 – 1.0 ng/mL as determined by the dose-dependent stimulation of HT-2 cell proliferation.

The specific activity of recombinant human IL-2 is approximately 2.36 x 104 IU/μg when compared against the 2nd WHO International Standard for Human IL-2 (NIBSC code: 86/500) as determined by dose-dependent stimulation of HT-2 cell proliferation.
Application

Bioassay

Application Notes

This IL-2 protein is biologically active and can be used for in vitro assays.


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 validated 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. Wingender G, et al. 2011. J. Exp. Med. 208:1151. PubMed
Product Citations
  1. Malu D, et al. 2011. J Immunol. 186:6271. PubMed
  2. Jiao S, et al. 2017. Clin Cancer Res. 23:3711. PubMed
  3. Liu Y, et al. 2018. JCI Insight. 3:. PubMed
Publication Library

Antigen Details

Structure
Cytokine
Distribution

Activated T cells

Function
IL-2 works in vivo to promote clonal T-cell expansion during immune responses. IL-2 stimulates the growth, differentiation, and survival of the Ag-selected cytotoxic T lymphocytes (CTLs). In addition, IL-2 regulates facilitate the proliferation and the synthesis of immunoglobulin by B cells, induces the generation and persistence of natural killer (NK) cells. Also, IL-2, through its role in activation-induced cell death (AICD) and its participation in the maintenance of peripheral CD4+CD25+ regulatory T (TReg) cells, is involved in the elimination of self-reactive T cells, which have a role in the pathogenesis of autoimmune diseases.
Interaction
T cells, B cells, NK cells, LAK cells, monocytes, macrophages, oligodendrocytes
Ligand Receptor
IL-2R is composed of three subunits, IL-2R alpha (p55, Tac Ag, or CD25), IL-2R beta (p75 or CD122), and the γc chain (p65 or CD132).
Cell Type
Hematopoietic stem and progenitors, Embryonic Stem Cells
Biology Area
Immunology, Stem Cells
Molecular Family
Cytokines/Chemokines
Antigen References

1. Smith KA. 1988. Science 240:1169.
2. D’Cruz LM, et al. 2005. Nature Immunol. 6:1152.
3. Maloy KJ, et al. 2005. Nature Immunol. 6:1071.
4. Waldmann TA. 2006. Nature Rev. Immunol. 6:595.
5. Ma A, et al. 2006. Annu. Rev. Immunol. 24:657.
6. Du J, et al. 2010. J. Immunol. 184:1361.

Gene ID
3558 View all products for this Gene ID
UniProt
View information about IL-2 on UniProt.org

Related FAQs

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.

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.

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)
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.

Go To Top Version: 9    Revision Date: 05/20/2019

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.

 

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