Purity
>90%, 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 by its ability to block human IL-15-induced proliferation of CTLL‑2 mouse cytotoxic T cells. Ruchatz, H. et al. (1998) J. Immunol. 160:5654. The ED 50 for this effect is 0.1-0.5 ng/mL in the presence of 0.1 ng/mL recombinant human IL-15.
Source
Mouse myeloma cell line, NS0-derived
Mouse IL-15 R alpha
(Gly33 - Lys205)
Accession # Q60819IEGRMD Human IgG1
(Pro100 - Lys330)N-terminus C-terminus Contains a small amount (10%) of free IL-15 R alpha and Fc generated by proteolytic cleavage.
Accession #
N-terminal Sequence
AnalysisGly33
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
44.9 kDa (monomer)
SDS-PAGE
80-90 kDa, 42 kDa and 35 kDa, reducing conditions
551-MR |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 100 μg/mL in sterile 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.
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Background: IL-15 R alpha
Interleukin 15 Receptor alpha (IL 15 R alpha ), also known as CD215, is a widely expressed 60 kDa transmembrane glycoprotein that plays an important role in the homeostasis and activation of NK cells and CD8+ memory T cells and participates in the development and function of many other hematopoietic cell types and non‑immune cell types (1 ‑ 3). Mature mouse IL‑15 R alpha consists of a 173 aa extracellular domain (ECD) containing one N‑linked glycosylation site, a 21 aa transmembrane segment, and a 37 aa cytoplasmic tail (4). Within the ECD, mouse IL‑15 R alpha shares 59% and 89% aa sequence identity with human and rat IL‑15 R alpha, respectively. Alternate splicing of mouse IL‑15 R alpha generates additional isoforms with an N‑terminal truncation or variable length deletions in the ECD. IL‑15 R alpha binds to Interleukin‑15 with high affinity (4). IL‑15 additionally interacts 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, 6). The use of shared receptor components contributes to the overlapping biological effects of IL‑15 and IL‑2. The dominant mechanism of IL‑15 action is known as transpresentation in which IL‑15/IL‑15 R alpha complexes are 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 (8 ‑ 10). IL‑15/IL‑15 R alpha complexes can transmit reverse signaling that promotes cellular adhesion, tyrosine phosphorylation of intracellular proteins, and cytokine secretion by the IL‑15/IL‑15 R alpha expressing cells (11, 12). Shed soluble forms of IL‑15 R alpha retain the ability to bind tightly to IL‑15 and can inhibit IL‑15 bioactivity (4, 13, 14).
References:
Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
Di Sabatino, A. et al. (2011) Cytokine Growth Factor Rev. 22:19.
Budagian, V. et al. (2006) Cytokine Growth Factor Rev. 17:259.
Giri, J.G. et al. (1995) EMBO 14:3654.
Grabstein, K. et al. (1994) Science 264:965.
Giri, J. et al. (1994) EMBO J. 13:2822.
Stonier, S.W. and K.S. Schluns (2010) Immunol. Lett. 127:85.
Duitman, E.H. et al. (2008) Mol. Cell. Biol. 28:4851.
Dubois, S. et al. (2002) Immunity 17:537.
Burkett, P.R. et al. (2004) J. Exp. Med. 200:825.
Budagian, V. et al. (2004) J. Biol. Chem. 279:42192.
Neely, G.G. et al. (2004) J. Immunol. 172:4225.
Budagian, V. et al. (2004) J. Biol. Chem. 279:40368.
Mortier, E. et al. (2004) J. Immunol. 173:1681.
Long Name:
Interleukin 15 Receptor alpha
Entrez Gene IDs:
3601 (Human); 16169 (Mouse)
Alternate Names:
CD215 antigen; CD215; IL-15 R alpha; IL-15 receptor subunit alpha; IL15R alpha; IL15RA; IL-15Ra; IL-15R-alpha; interleukin 15 receptor, alpha; interleukin-15 receptor subunit alpha; MGC104179
