Anti-Human IL-15 Receptor Purified

Description: The eBioJM7A4 monoclonal antibody reacts with the IL-15 receptor alpha chain (IL-15Rα). IL-15 and IL-2 are cytokines with overlapping, but distinct, biologic effects. Their receptors share 2 subunits, the IL2R-β and -γ chains, which are essential for signal transduction. The IL-15R-α receptor is structurally related to IL-2R-α. However, the IL-15Rα alone binds IL-15 with a 1,000-fold higher affinity than that seen with IL-2R-α and IL-2. In the human, 3 differentially spliced human IL15R-α variants that are all capable of high affinity binding of IL-15 have been isolated. The cytoplasmic domain of IL15R-α, like that of IL2R-α, is dispensable for mitogenic signaling, suggesting that the primary role of the alpha chains is to confer high affinity binding. At high concentrations, IL-15, like IL-2, is able to signal through a complex of IL2R-β and IL2R-γ in the absence of the alpha subunit.

References: Vamosi G, Bodnar A, Vereb G, Jenei A, Goldman CK, Langowski J, Toth K, Matyus L, Szollosi J, Waldmann TA, Damjanovich S. IL-2 and IL-15 receptor alpha-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells.Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):11082-7. (JM7A4, FRET, PubMed)

Dubois S, Mariner J, Waldmann TA, Tagaya Y. IL-15Ralpha recycles and presents IL-15 In trans to neighboring cells.Immunity. 2002 Nov;17(5):537-47. (JM7A4, FC, WB, PubMed)

Anderson, D., et al. 1995. Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes. J. Biol. Chem. 270: 29862-29869.

Giri, J., et al. 1995. Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha of the IL-2 receptor. EMBO J. 14: 3654-3663.