Recombinant Human IL-15 Hyperactive Protein, CF

R&D Systems | Catalog # BT-015H

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Key Product Details

Source

E. coli

Applications

Bioactivity
View all IL-15 Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human IL-15 protein
Proprietary, engineered based on P40933

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Predicted Molecular Mass


SDS-PAGE

9-11 kDa, under reducing conditions.

Activity

Measured in a cell proliferation assay using NK-92 human natural killer lymphoma cells.
The ED50 for this effect is 0.0300-0.300 ng/mL.

Scientific Data Images for Recombinant Human IL-15 Hyperactive Protein, CF

Recombinant Human IL‑15 Hyperactive Protein Bioactivity.

The Recombinant Human IL‑15 Hyperactive Protein (Catalog # BT-015H) induces proliferation of NK-92 human natural killer lymphoma cells.

Recombinant Human IL‑15 Hyperactive Protein SDS-PAGE.

2 μg/lane of Recombinant Human IL‑15 Hyperactive Protein (Catalog # BT-015H) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 9-11 kDa, under reducing conditions.

Formulation, Preparation, and Storage

BT-015H
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 100 μg/mL in 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: IL-15

Interleukin 15 (IL-15) is a widely expressed 14 kDa cytokine that is structurally and functionally related to IL-2 and plays an important role in many immunological diseases (1, 2). Mature human IL-15 shares 70% amino acid sequence identity with mouse and rat IL-15. Alternative splicing generates isoforms of IL-15 with either a long or short signal peptide (LSP or SSP), and the SSP isoform is retained intracellularly (3). IL-15 binds with high affinity to IL-15 R alpha (4). It binds with lower affinity to a complex of IL-2 R beta and the common gamma chain ( gamma c) which are also subunits of the IL-2 receptor complex (5). IL-15 associates with IL-15 R alpha in the endoplasmic reticulum, and this complex is expressed on the cell surface (6). The dominant mechanism of IL-15 action is known as transpresentation in which IL-15 and IL-15 R alpha are coordinately expressed on the surface of one cell and interact with complexes of IL-2 R beta / gamma c on adjacent cells (7). This enables cells to respond to IL-15 even if they do not express IL-15 R alpha (6). In human and mouse, soluble IL-15-binding forms of IL-15 R alpha can be generated by proteolytic shedding and bind up nearly all the IL-15 in circulation (8-10). Soluble IL-15 R alpha functions as an inhibitor that limits IL-15 action (4, 9). Ligation of membrane-associated IL-15/IL-15 R alpha complexes also induces reverse signaling that promotes activation of the IL-15/IL-15 R alpha expressing cells (11). IL-15 induces or enhances the differentiation, maintenance, or activation of multiple T cell subsets including NK, NKT, Th17, Treg, and CD8+ memory cells (12 - 16). An important component of these functions is the ability of IL‑15 to induce dendritic cell differentiation and inflammatory activation (11, 14). IL-15 exhibits anti-tumor activity independent of its actions on NK cells or CD8+ T cells (17). It also inhibits the deposition of lipid in adipocytes, and its circulating levels are decreased in obesity (18). Immunotherapy treatment with recombinant IL-15 has the advantage of not stimulating Treg cells like IL-2 does but has the drawback of associated toxicity at higher doses. This has led to increased investigation on mitigating IL-15 toxicity and combination immunotherapy approaches using immune checkpoint inhibitors (19, 20). Preclinical and early clinical studies have shown the potential of also using IL-15 in combination with cancer vaccines to improve their anti-tumor response (20). IL-15 can also be used for the preconditioning of CAR T cells or for engineering cells to express IL-15 in vivo. Adoptive cell transfer of NK cells engineered to express CD19 and IL-15 were well tolerated in patients with CD19-positive cancers (20). IL-15 can be used in combination with other cytokines like IL-21 to increase the efficiency of NK cell expansion and maturation in stem cell culture protocols (21). The combination of IL-15 with IL-7 also promotes expansion of early-differentiated CD8+ T cells in culture with the added benefit of decreasing Treg cell generation, unlike IL-2, for adoptive cell transfer in cancer immunotherapy (22). GMP IL-7 and GMP IL-15 are commonly used in combination for ex vivo expansion of T cells for cellular therapies.rhIL-15 Hyperactive is engineered for increased affinity to IL-15R beta and IL-15R alpha, making it a more potent cytokine ideal for expanding challenging cells like TILs and NK cells that require extended ex vivo culture.

References

  1. De Sabatino, A. et al. (2011) Cytokine Growth Factor Rev. 22:19.
  2. Grabstein, K. et al. (1994) Science 264:965.
  3. Tagaya, Y. et al. (1997) Proc. Natl. Acad. Sci. USA 94:14444.
  4. Giri, J.G. et al. (1995) EMBO J. 14:3654.
  5. Giri, J. et al. (1994) EMBO J. 13:2822.
  6. Dubois, S. et al. (2002) Immunity 17:537.
  7. Castillo, E.F. and K.S. Schluns (2012) Cytokine 59:479.
  8. Budagian, V. et al. (2004) J. Biol. Chem. 279:40368.
  9. Mortier, E. et al. (2004) J. Immunol. 173:1681.
  10. Bergamaschi, C. et al. (2012) Blood 120:e1.
  11. Budagian, V. et al. (2004) J. Biol. Chem. 279:42192.
  12. Mortier, E. et al. (2003) J. Exp. Med. 205:1213.
  13. Gordy, L.E. et al. (2011) J. Immunol. 187:6335.
  14. Harris, K.M. (2011) J. Leukoc. Biol. 90:727.
  15. Xia, J. et al. (2010) Clin. Immunol. 134:130.
  16. Schluns, K.S. et al. (2002) J. Immunol. 168:4827.
  17. Davies, E. et al. (2010) J. Leukoc. Biol. 88:529.
  18. Barra, N.G. et al. (2010) Obesity 18:1601.
  19. Xue, D. et al. (2021) Antib Ther. 4:123.
  20. Wolfarth, A.A. et al. (2022) Immune Netw. 22:e5.
  21. Oberoi, P. et al. (2020). Cells. 9:811.
  22. Chamucero-Millares, J.A. et al. (2021) Cellular Immunol. 360:104257.

Long Name

Interleukin 15

Alternate Names

IL15

Entrez Gene IDs

3600 (Human); 16168 (Mouse); 25670 (Rat); 102119613 (Cynomolgus Monkey); 493682 (Feline)

Gene Symbol

IL15

Additional IL-15 Products

Product Documents for Recombinant Human IL-15 Hyperactive Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human IL-15 Hyperactive Protein, CF

For research use only

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