Recombinant Human IL-2 Protein

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Recombinant Human IL-2 (Catalog # 202-IL) stimulates cell proliferation of the CTLL‑2 mouse cytotoxic T cell line. The ED50 for this effect is 0.0500-0.250 ng/mL.
1 μg/lane of Recombinant Human IL-2 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 13 kDa.
As an alternative, please consider our next generation Recombinant Human IL-2 (BT-002). It has equivalent bioactivity to Recombinant Human IL-2 (Catalog # 202-IL). It combines R&D Systems quality with scalability that ...read more
Equivalent bioactivity of GMP (202-GMP), Animal-Free (AFL202) and RUO (Catalog # 202-IL) grades of Recombinant Human IL-2 as measured in a cell proliferation assay CTLL 2 mouse cytotoxic T cells (orange, green, red, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human IL-2 Protein Summary

Details of Functionality
Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. Gearing, A.J.H. and C.B. Bird (1987) in Lymphokines and Interferons, A Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 295. The ED50 for this effect is 0.0500-0.250 ng/mL.
Source
E. coli-derived human IL-2 protein
Ala21-Thr153, with an N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Gene
IL2
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
15 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
13 kDa, under reducing conditions.
Publications
Read Publications using
202-IL in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 100 mM Acetic Acid containing at least 0.1% human or bovine serum albumin.  Alternatively, reconstitute at 100 μg/mL in sterile deionized water and use within 24 hours, store at 2 to 8 °C.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-2 Protein

  • Aldesleukin
  • IL2
  • IL-2
  • IL-2lymphokine
  • interleukin 2
  • interleukin-2
  • involved in regulation of T-cell clonal expansion
  • Proleukin
  • T cell growth factor
  • T-cell growth factor
  • TCGF

Background

Recombinant Interleukin-2 (IL-2) is expressed in E. coli and has been engineered to contain the serine for cysteine substitution found in Proleukin® (aldesleukin). Recombinant IL-2 is widely used in cell culture for the expansion of T cells. IL-2 is expressed by CD4+ and CD8+ T cells, gamma δ T cells, B cells, dendritic cells, and eosinophils (1-3). Mature human IL-2 shares 56% and 66% amino acid (aa) sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit cross-species activity (4). The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes (5-7). The 55 kDa IL-2 R alpha is specific for IL-2 and binds with low affinity. The 75 kDa IL-2 R beta , which is also a component of the IL-15 receptor, binds IL-2 with intermediate affinity. The 64 kDa common gamma chain gamma c/IL-2 R gamma , which is shared with the receptors for IL-4, -7, -9, -15, and -21, does not independently interact with IL-2. Upon ligand binding, signal transduction is performed by both IL-2 R beta and gamma c.

IL-2 is best known for its autocrine and paracrine activity on T cells. It drives resting T cells to proliferate and induces IL-2 and IL-2 R alpha synthesis (1, 2). It contributes to T cell homeostasis by promoting the Fas-induced death of naïve CD4+ T cells but not activated CD4+ memory lymphocytes (8). IL-2 plays a central role in the expansion and maintenance of regulatory T cells, although it inhibits the development of Th17 polarized cells (9-11). Thus, IL-2 may be a key cytokine in the natural suppression of autoimmunity (12, 13).

IL-2 expression and concentration can have either immunostimulatory effects at high doses or immunosuppressive effects at low doses due to its preferential binding to different receptor subunits expressed by various immune cell types. This has led to the generation of recombinant IL-2 variants aimed at modifying IL-2 receptor binding for increased antitumor efficacy (14, 15). These variants are typically used in combination with immune checkpoint inhibitors instead of as a monotherapy (14). IL-2 can be genetically engineered to express in NK cells for CAR T cell therapies, and in combination with other cytokines like IL-15, can increase cell viability and proliferation (16). In addition to adoptive cell transfer and checkpoint blockade inhibitors, cancer vaccines that boost immune responses have been combined with IL-2 treatment with promising results in recent studies (15).

In cell culture, IL-2 is a frequently used cytokine for the proliferation, differentiation, and increased antibody secretion of B cells as they transform into plasma cells in vitro (17). IL-2 is also a classically used cytokine for the expansion of NK cells, early differentiated T cells and effector memory Treg cells for adoptive cell transfer cancer immunotherapy (16, 18). GMP IL-2 is a commonly used supplement for the expansion of these cell types for cellular therapies.

  1. Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
  2. Gaffen, S.L. and K.D. Liu (2004) Cytokine 28:109.
  3. Taniguchi, T. et al. (1983) Nature 302:305.
  4. Mosmann, T.R. et al. (1987) J. Immunol. 138:1813.
  5. Liparoto, S.F. et al. (2002) Biochemistry 41:2543.
  6. Wang, X. et al. (2005) Science 310:1159.
  7. Bodnar, A. et al. (2008) Immunol. Lett. 116:117.
  8. Jaleco, S. et al. (2003) J. Immunol. 171:61.
  9. Malek, T.R. (2003) J. Leukoc. Biol. 74:961.
  10. Laurence, A. et al. (2007) Immunity 26:371.
  11. Kryczek, I. et al. (2007) J. Immunol. 178:6730.
  12. Afzali, B. et al. (2007) Clin. Exp. Immunol. 148:32.
  13. Fehervari, Z.et al. (2006) Trends Immunol. 27:109.
  14. Xue, D. et al. (2021) Antibody Therapeutics. 4(2): 123-133.
  15. Wolfarth, A.A. et al. (2022) Immune Netw. 22(1): e5.
  16. Koehl, U. et al. (2015) Oncoimmunology. 5(4).
  17. Marsman, C. et al. (2022) Front. In Immunol. 13(815449).
  18. Chamucero-Millares, J.A. et al. (2021) Cellular Immunology. 360(104257).

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Publications for IL-2 (202-IL)(352)

We have publications tested in 10 confirmed species: Human, Mouse, Bat - Pteropus alecto, Bovine, Canine, Chinchilla, Complex Species Category, Feline, N/A, Primate - Macaca mulatta (Rhesus Macaque).

We have publications tested in 9 applications: Bioassay, CAR-T, CAR-T (Bioassay), CAR-T (Differentiation), Cell Culture, ELISA (Standard), In Vivo, Luminex Development, Surface Plasmon Resonance.


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Bioassay
(307)
CAR-T
(1)
CAR-T (Bioassay)
(2)
CAR-T (Differentiation)
(1)
Cell Culture
(32)
ELISA (Standard)
(3)
In Vivo
(2)
Luminex Development
(1)
Surface Plasmon Resonance
(1)
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Human
(300)
Mouse
(40)
Bat - Pteropus alecto
(1)
Bovine
(1)
Canine
(1)
Chinchilla
(1)
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(1)
Feline
(1)
N/A
(3)
Primate - Macaca mulatta (Rhesus Macaque)
(2)
All Species
Showing Publications 1 - 10 of 352. Show All 352 Publications.
Publications using 202-IL Applications Species
G Silva, AF Rodrigues, S Ferreira, C Matos, RP Eleutério, G Marques, K Kucheryava, AR Lemos, PMF Sousa, R Castro, A Barbas, D Simão, PM Alves Novel scFv against Notch Ligand JAG1 Suitable for Development of Cell Therapies toward JAG1-Positive Tumors Biomolecules, 2023;13(3):. 2023-01-01 [PMID: 36979394] (Bioassay, Human) Bioassay Human
R Boytz, S Seitz, E Gaudiano, JJ Patten, PT Keiser, JH Connor, AH Sharpe, RA Davey Inactivation of Ebola Virus and SARS-CoV-2 in Cell Culture Supernatants and Cell Pellets by Gamma Irradiation Viruses, 2022;15(1):. 2022-01-01 [PMID: 36680083] (Bioassay, Complex Species Category) Bioassay Complex Species Category
ACH Szeto, ACF Ferreira, J Mannion, PA Clark, M Sivasubram, MWD Heycock, A Crisp, HE Jolin, P Kozik, MD Knolle, ANJ McKenzie An alphavbeta3 integrin checkpoint is critical for efficient TH2 cell cytokine polarization and potentiation of antigen-specific immunity Nature Immunology, 2023;24(1):123-135. 2023-01-01 [PMID: 36550322] (Bioassay, Human) Bioassay Human
MJ Lee, MW Leong, A Rustagi, A Beck, L Zeng, S Holmes, LS Qi, CA Blish SARS-CoV-2 escapes direct NK cell killing through Nsp1-mediated downregulation of ligands for NKG2D Cell Reports, 2022;41(13):111892. 2022-01-01 [PMID: 36543165] (Cell Culture, Human) Cell Culture Human
E Cruz-Loren, NP Ramirez, J Lee, S Pandhe, L Wang, J Hernandez-, AM Spivak, V Planelles, T Petersen, MK Jain, ED Martinez, I D'Orso Host Cell Redox Alterations Promote Latent HIV-1 Reactivation through Atypical Transcription Factor Cooperativity Viruses, 2022;14(10):. 2022-01-01 [PMID: 36298843] (Bioassay, Human) Bioassay Human
WE Jiao, S Xu, YL Qiao, YG Kong, L Sun, YQ Deng, R Yang, ZZ Tao, QQ Hua, SM Chen Notch2-dependent GATA3+ Treg cells alleviate allergic rhinitis by suppressing the Th2 cell response International immunopharmacology, 2022;112(0):109261. 2022-01-01 [PMID: 36155282] (Bioassay, Human) Bioassay Human
B Noailly, M Yaugel-Nov, J Werquin, F Jospin, D Drocourt, T Bourlet, N Rochereau, S Paul Antiviral Activities of HIV-1-Specific Human Broadly Neutralizing Antibodies Are Isotype-Dependent Vaccines, 2022;10(6):. 2022-01-01 [PMID: 35746511] (Bioassay, Human) Bioassay Human
Somasundaram A, Cillo A, Lampenfeld C, Workman C, Kunning S, Oliveri L, Velez M, Joyce S, Calderon M, Dadey R, Rajasundaram D, Normolle D, Watkins S, Herman J, Kirkwood J, Lipson E, Ferris R, Bruno T, Vignali D Systemic Immune Dysfunction in Cancer Patients Driven by IL6 Induction of LAG3 in Peripheral CD8+ T Cells. Cancer Immunol Res, 0;10(7):885-899. [PMID: 35587532] (Bioassay, Human) Bioassay Human
G Rodionov, M Rosenzwaig, MS Tzadok, M Kvint, E Gevir, E Zorde-Khva, A Peled, S Yarkoni, A Ofer Short treatment of peripheral blood cells product with Fas ligand using closed automated cell processing system significantly reduces immune cell reactivity of the graft in vitro and in vivo Bone marrow transplantation, 2022;0(0):. 2022-01-01 [PMID: 35538142] (Bioassay, Human) Bioassay Human
CA Robinson, TD Lyddon, HM Gil, DT Evans, YV Kuzmichev, J Richard, A Finzi, S Welbourn, L Rasmussen, NM Nebane, VV Gupta, S Ananthan, Z Cai, ER Wonderlich, CE Augelli-Sz, R Bostwick, RG Ptak, SM Schader, MC Johnson Novel Compound Inhibitors of HIV-1NL4-3 Vpu Viruses, 2022;14(4):. 2022-01-01 [PMID: 35458546] (Bioassay, Human) Bioassay Human
Show All 352 Publications.

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FAQs for IL-2 (202-IL). (Showing 1 - 1 of 1 FAQs).

  1. we bought the rHIL-2 protein ref 202-IL-500 and it says that the reconstitution has to be done in acetic acid, but I need to use the protein in PBS, is that possible to reconstitute it directly in PBS instead? would it be stable?
    • It will not be soluble in PBS alone so 100 mM acetic acid is required for it to go into solution. Then you can dilute into PBS only and that should not affect your experimentation.

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Bioinformatics

Gene Symbol IL2
Uniprot