Recombinant Human IL-2 (Cys145Ser) Protein

Newer Version Available: BT-002
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Discontinued Product

1081-IL has been discontinued and is replaced by BT-002.

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Recombinant Human IL-2 (Cys145Ser) Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 0.05-0.25ng/mL.
Source
E. coli-derived human IL-2 protein
Ala21-Thr153 (Cys145Ser), with and without an N-terminal Met
Accession #
N-terminal Sequence
Analysis
Ala21 & Met
Predicted Molecular Mass
15.5 kDa

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1081-IL (with carrier)

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1081-IL/CF (carrier free)

Discontinued Product

1081-IL

Formulation Lyophilized from a 0.2 μm filtered solution in Sodium Acetate with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: IL-2

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.

References
  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).
Long Name
Interleukin 2
Entrez Gene IDs
3558 (Human); 16183 (Mouse); 116562 (Rat); 396868 (Porcine); 280822 (Bovine); 403989 (Canine); 100034204 (Equine); 751114 (Feline); 100302458 (Rabbit)
Alternate Names
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

Citations for Recombinant Human IL-2 (Cys145Ser) Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Super-enhancer-based identification of a BATF3/IL-2R-module reveals vulnerabilities in anaplastic large cell lymphoma
    Authors: HC Liang, M Costanza, N Prutsch, MW Zimmerman, E Gurnhofer, IA Montes-Moj, BJ Abraham, N Prokoph, S Stoiber, S Tangermann, C Lobello, J Oppelt, I Anagnostop, T Hielscher, S Pervez, W Klapper, F Zammarchi, DA Silva, KC Garcia, D Baker, M Janz, N Schleussne, F Fend, Š Pospíšilov, A Janiková, J Wallwitz, D Stoiber, I Simonitsch, L Cerroni, S Pileri, L de Leval, D Sibon, V Fataccioli, P Gaulard, C Assaf, F Knörr, C Damm-Welk, W Woessmann, SD Turner, AT Look, S Mathas, L Kenner, O Merkel
    Nature Communications, 2021-09-22;12(1):5577.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  2. An HLA-A2.1-transgenic rabbit model to study immunity to papillomavirus infection.
    Authors: Hu J, Peng X, Schell TD, Budgeon LR, Cladel NM, Christensen ND
    J. Immunol., 2006-12-01;177(11):8037-45.
    Species: Rabbit
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Human plasmacytoid predendritic cells activate NK cells through glucocorticoid-induced tumor necrosis factor receptor-ligand (GITRL).
    Authors: Hanabuchi S, Watanabe N, Wang YH, Ito T, Shaw J, Cao W, Qin FX, Liu YJ
    Blood, 2006-01-05;107(9):3617-23.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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