TRAIL (TNFSF10) selectively induces apoptosis in transformed cells while sparing most normal cell types, making it a critical tool for dissecting death receptor signaling in cancer biology. This tag-free recombinant human TRAIL, spanning residues 115–281, demonstrates potent cytotoxicity with an ED50 of 1–10 ng/ml in actinomycin D-sensitized L-929 fibroblasts, confirming robust activation of the extrinsic apoptosis cascade. The protein supports use in tumor cell apoptosis assays, DR4/DR5 receptor signaling studies involving caspase and NF-κB pathway activation, in vivo tumor biology models, and as a reference standard for TRAIL detection assays. Endotoxin levels below 1.0 EU/μg minimize LPS-driven artifacts in immune cell experiments, while purity exceeding 95% by SDS-PAGE provides a suitable basis for antibody development and validation workflows including immunogen preparation and ELISA controls.
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