Recombinant Human Tumor necrosis factor ligand superfamily member 11 (TNFSF11), partial (Active)

RANKL is the principal cytokine driving osteoclast differentiation and a key activator of NF-κB signaling, making it indispensable in bone biology and tumor microenvironment research. This recombinant human TNFSF11 partial protein (residues 63–244 of Isoform 2), expressed in mammalian cells with an N-terminal 6xHis tag, demonstrates strong binding to its decoy receptor osteoprotegerin (TNFRSF11B) with an EC50 of 4.514–5.152 ng/mL in functional ELISA, confirming signaling-competent conformation suitable for osteoclast differentiation assays, NF-κB pathway activation studies, and use as a coating antigen or positive control in antibody development workflows. Purity exceeding 95% by SDS-PAGE and endotoxin levels below 1.0 EU/μg satisfy the stringent criteria needed to prevent LPS-driven artifacts in primary monocyte and macrophage precursor cultures. These specifications also provide a suitable basis for in vivo tumor biology models where RANKL-mediated signaling influences metastatic bone disease.