CD215 (IL-15Ra) Monoclonal Antibody (eBioJM7A4), eBioscience™, Invitrogen™

Description

• The eBioJM7A4 MAb reacts with the IL-15 receptor alpha chain (IL-15Ralpha)
• IL-15 and IL-2 are cytokines with overlapping, but distinct, biologic effects
• Their receptors share 2 subunits, the IL-2Rbeta and gamma chains, which are essential for signal transduction
• The IL-15Ralpha receptor is structurally related to IL-2Ralpha
• However, the IL-15Ralpha alone binds IL-15 with a 1,000-fold higher affinity than that seen with IL-2Ralpha and IL-2
• In the human, 3 differentially spliced human IL-15Ralpha variants that are all capable of high affinity binding of IL-15 have been isolated
• The cytoplasmic domain of IL-15Ralpha, like that of IL-2Ralpha, 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 IL-2Rbeta and IL-2Rgamma in the absence of the alpha subunit
• Interleukin 15 (IL-15RA) is a cytokine receptor that specifically binds IL-15 with high affinity
• IL-15 regulates T and natural killer cell activation and proliferation
• The IL-15 and IL-2 receptors share two subunits, IL-2R beta and IL-2R gamma, and IL-15RA is structurally related to IL-2RA, an additional IL-2-specific alpha subunit necessary for high affinity IL-2 binding
• Unlike IL-2RA, IL-15RA is capable of binding IL-15 with high affinity independent of the other subunits
• IL-15RA is thought to enhance cell proliferation and expression of apoptosis inhibitor Bcl-xL and Bcl-2.