Biotinylated IL-15 R alpha His&Avi Tag Protein, Human

IL-15Rα (Interleukin-15 receptor alpha chain) is a type I transmembrane glycoprotein and a member of the cytokine receptor superfamily. Its extracellular domain contains a sushi domain (also known as a complement control protein module), which is responsible for high-affinity binding to IL-15. This receptor does not transmit signals on its own; instead, it forms a functional IL-15 receptor complex together with the IL-2/15Rβ (CD122) and γc (CD132) chains.The core biological function of IL-15Rα lies in its trans-presentation mechanism, through which it anchors IL-15 onto the surface of dendritic cells, monocytes, or stromal cells, forming a stable IL-15/IL-15Rα complex. This complex specifically activates NK cells, CD8⁺ memory T cells, and innate lymphoid cells (ILCs), supporting their survival, proliferation, and cytotoxic functions. Additionally, membrane-bound IL-15Rα can be cleaved by matrix metalloproteinases (MMPs) to generate a soluble form, which acts as an endogenous antagonist of IL-15 and participates in immune regulation.IL-15Rα is a key target in cancer immunotherapy—superagonists (e.g., N-803/ALT-803) and recombinant proteins (e.g., NIZ985) based on the IL-15/IL-15Rα heterodimer have entered clinical trials. These agents enhance antitumor immunity by expanding NK cells and cytotoxic T cells, and show synergistic effects when combined with PD-1/PD-L1 inhibitors. Meanwhile, soluble IL-15Rα plays a negative regulatory role in autoimmune diseases such as psoriasis, offering new intervention strategies for inflammatory diseases.