Recombinant Human IL-15 GMP Protein, CF

Animal-Free.
  
  • Purity
    >97%, by SDS-PAGE with silver staining, under reducing conditions.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 for this effect is 0.3-2.6 ng/mL.
    The specific activity of recombinant human IL-15 is approximately 4.5 x 105 U/μg, which is calibrated against recombinant human IL-15 WHO Standard (NIBSC code: 95/554).
  • Source
    E. coli-derived Asn49-Ser162 Produced using non-animal reagents in an animal-free laboratory.
    Manufactured and tested under current Good Manufacturing Practice (GMP) guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis
    Asn-Trp-Val-Asn-Val-Ile-Ser-Asp-Leu-Lys
  • Predicted Molecular Mass
    12.5 kDa
247-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in PBS.
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.
  • A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Data Images

GMP-grade Recombinant Human IL-15 (Catalog # 247-GMP) stimulates cell proliferation in the MO7e human megakaryocytic leukemic cell line. The ED50 for this effect is 0.3-2.6 ng/mL.

1 μg/lane of GMP-grade Recombinant Human IL-15 (Catalog # 247-GMP) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 12 kDa.

Mass Spectrometry

MALDI-TOF analysis of GMP-grade Recombinant Human IL-15 (Catalog #
247-GMP). The major peak corresponds to the calculated molecular mass, 12774 Da. The minor peak at 13006 Da is a matrix-associated artifact of the MALDI-TOF.

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).
  • 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.
  • Long Name:
    Interleukin 15
  • Entrez Gene IDs:
    3600 (Human); 16168 (Mouse); 25670 (Rat); 493682 (Feline)
  • Alternate Names:
    IL15; IL-15; IL-15MGC9721; interleukin 15; interleukin-15

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