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Recombinant Human IL-2 Protein, CF Best Seller

R&D Systems, part of Bio-Techne | Catalog # BT-002

Contains the Cysteine to Serine substitution found in Proleukin® (aldesleukin)
R&D Systems, part of Bio-Techne
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BT-002-010
BT-002-01M
BT-002-050
BT-002-100
BT-002-500

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

E. coli-derived human IL-2 protein
Ala21-Thr153 (Cys145Ser), with and without an N-terminal Met

Purity

>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ala21 & Met

Predicted Molecular Mass

15.5 kDa

SDS-PAGE

13 kDa, under reducing conditions.

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 0.0300-0.250 ng/mL.

Scientific Data Images for Recombinant Human IL-2 Protein, CF

Recombinant Human IL‑2 Protein Bioactivity.

Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is 0.0300-0.250 ng/mL.

Equivalent Bioactivity of GMP, Animal-Free, and RUO grades of Recombinant Human IL-2.

Equivalent bioactivity of GMP (BT-002-GMP), Animal-Free (BT-002-AFL) and RUO (Catalog # BT-002) grades of Recombinant Human IL-2 as measured in a cell proliferation assay using CTLL-2 mouse cytotoxic T cells (orange, green, red, respectively).

Recombinant Human IL‑2 Protein SDS-PAGE.

2 μg/lane of Recombinant Human IL‑2 Protein (Catalog # BT-002) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 13 kDa.

Formulation, Preparation and Storage

BT-002
Formulation Lyophilized from a 0.2 μm filtered solution in Sodium Acetate with Trehalose.
Reconstitution Reconstitute the 10 μg size at 100 μg/mL in sterile deionized water. Reconstitute all other sizes at 500 μg/mL in sterile deionized water.
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.

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 delta 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 gammac/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 gammac. 

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) Antib Ther. 4:123.
  15. Wolfarth, A.A. et al. (2022) Immune Netw. 22:e5.
  16. Koehl, U. et al. (2015) Oncoimmunology. 5:e1115178.
  17. Marsman, C. et al. (2022) Front. In Immunol. 13:815449.
  18. Chamucero-Millares, J.A. et al. (2021) Cellular Immunol. 360:104257.

Long Name

Interleukin 2

Alternate Names

Aldesleukin, IL2, Proleukin, TCGF

Entrez Gene IDs

3558 (Human); 16183 (Mouse); 116562 (Rat); 396868 (Porcine); 280822 (Bovine); 403989 (Canine); 100034204 (Equine); 751114 (Feline); 100302458 (Rabbit)

Gene Symbol

IL2

UniProt

Additional IL-2 Products

Product Documents for Recombinant Human IL-2 Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human IL-2 Protein, CF

Proleukin® is a registered trademark of Clinigen Holdings Limited.

For research use only

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