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Human IL-15, amino acids Asn49-Ser162 (Accession# NM_000585) was expressed in E. coli.
Molecular Mass:
The 114 amino acid recombinant protein has a predicted molecular mass of 12,773 Da. The DTT-reduced protein migrates at approximately 9kDa and the non-reduced protein migrates at approximately 7kDa by SDS-PAGE. The N-terminal amino acid is Asn.
Purity:
Purity is >98%, as determined by Coomassie stained SDS-PAGE.
Formulation:
0.22 µm filtered protein solution is in 10mM NaH2PO4, 150mM NaCl, pH 7.2.
Endotoxin Level:
Endotoxin level is <0.1 EU/µg (<0.01ng/µg) protein as determined by the LAL method.
Preparation:
10-100µg sizes are bottled at 200µg/mL. 500µg sizes and larger are bottled at the concentration indicated on the vial.
Storage & Handling:
Unopened vial can be stored at 4°C for three months, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10µg/mL in buffer containing carrier protein such as 1% BSA or HSA or 10% FBS. For long term storage, aliquot into polypropylene vials and store in a manual defrost freezer. Avoid repeated freeze/thaw cycles.
Activity:
ED50 is 0.10-0.50 ng/ml, corresponding to a specific activity of 2-10 x 106 units/mg, as determined by the dose dependent stimulation of CTLL-2 cells proliferation.
IL-15 was discovered in the supernatant from a simian kidney epithelial cell line CV-1/EBNA, as a soluble factor capable of supporting proliferation of the IL-2-dependent cell line, CTLL-2 (1). Interleukin-15 (IL-15) is a regulatory cytokine, and it is produced by dendritic cells, epithelial cells, human stromal cell line (IMTLH), fibroblasts, and monocytes (2). IL-15 plays an important role in immune response and shares many functions with IL-2, for example, stimulating the proliferation of activated T cells (1, 2), NK cells (3) and B cells, and inducing immunoglobulin synthesis by B cells stimulated by anti-IgM or CD40 ligand (4). In addition, IL-15 promotes the development of dendritic cells (5), activates human neutrophils (6, 7) and induces the production of proinflammatory cytokines from macrophages (8). IL-15 acts as a bridge between innate and adaptive immunity because of its diverse roles in the immune system. IL-15 binds to heterotrimeric receptors composed of IL-15Rα, IL-15Rβ, and IL-15Rγc. IL-15 shares with IL-2 the receptor chains β and γc. IL-15 is normally not secreted in soluble form but is held on the cell surface bound to a unique receptor, IL-15Rα, especially on dendritic cells. Cell-bound IL-15 then is presented in trans to T cells and NK cells and is recognized by the γc receptor on these cells; such recognition maintains cell survival and intermittent proliferation (9).
Other Names:
IL-15; MGC9721
Structure:
13 kD single non-glycosylated polypeptide
Distribution:
IL-15 is expressed by DC, epithelial cells, human stromal cell line (IMTLH), fibroblasts, and monocytes.
Function:
IL-15 stimulates the proliferation of activated T cells (1, 2), NK cells (3) and B cells, and inducing immunoglobulin synthesis by B cells stimulated by anti-IgM or CD40 ligand (4). In addition, IL-15 promotes the development of dendritic cells (5), activates human neutrophils (6, 7) and induces the production of proinflammatory cytokines from macrophages (8).
Cellular Sources:
adherent peripheral blood mononuclear cells, fibroblasts and epithelial cells
Cellular Targets:
T lymphocytes, NK cells
Receptors:
IL-15Rα, IL-15Rβ and IL-15γc
Bioactivity/Activities:
stimulatory activities on the proliferation, survival and activation of T lymphocytes and NK cells, and the pathogenesis of rheumatoid arthritis via activating T cells and induces IL-17 production
Antigen References:
1. Grabstein K, et al. Science 264:965-968 1994. 2. Ma A, et al. Annu Rev Immunol 24:657-679 2006. 3. Meresse B, et al. Immunity 21:357-366 2004. 4. Armitage RJ et al, J Immunol 154:483-490 1995. 5. Pulendran B, et al. Eur. J. Immunol. 34:66-73 2004. 6. Bouchard A, et al. J. Leukoc. Biol. 76:162-168 2004. 7. Ratthe C, et al. 2004. J. Leukoc. Biol. 75:893. 8.Feng T, et al. 2008. Cell Immunol 5:189. 9. Rubinstein MP et al, P. Natl. Acad. Sci. USA 103:9166-9171 2006.
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