Recombinant Human Interleukin-15 receptor subunit alpha (IL15RA), partial (Active)

IL-15 signaling drives NK cell and memory CD8+ T cell homeostasis, and this recombinant human IL15RA fragment (aa 31–172 of Isoform 2) provides the extracellular sushi domain responsible for high-affinity IL-15 binding, enabling precise interrogation of receptor-ligand interactions. Functional validation confirms an ED50 of 0.35–3.5 ng/mL in blocking IL-15-induced CTLL-2 proliferation, directly supporting use in competitive inhibition assays, blocking antibody screening, and biologic inhibitor discovery campaigns. Mammalian cell expression preserves native glycosylation and disulfide-mediated folding critical for conformational integrity, making this C-terminal Fc-tagged construct appropriate for SPR- or BLI-based affinity characterization, ELISA-format ligand-binding studies, and therapeutic antibody epitope mapping. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based functional assays and sensitive biophysical measurements.