TRAIL Human (114-281 a.a.), Active

The recombinant human TRAIL protein, specifically the fragment spanning amino acids 114 to 281, is produced in Escherichia coli. This fragment is a non-glycosylated polypeptide chain containing 168-169 amino acids, with a molecular mass of approximately 19.6 to 21 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity (>95%) and low endotoxin levels (<0.1 EU/µg) .

TRAIL induces apoptosis by binding to its receptors on the cell surface. It interacts with several receptors, including TRAIL-R1 (DR4) and TRAIL-R2 (DR5), which contain death domains that initiate the apoptotic signaling cascade. Additionally, TRAIL can bind to decoy receptors such as TRAIL-R3 (DcR1) and TRAIL-R4 (DcR2), which do not induce apoptosis but can modulate the activity of TRAIL by competing for binding .

The recombinant TRAIL protein is biologically active and has been shown to induce apoptosis in various cell lines, including U937 cells and thyroid carcinoma lines, at concentrations ranging from 0.5 to 2.0 µg/mL . This activity is crucial for its potential therapeutic applications in cancer treatment, as it can selectively induce cell death in tumor cells while sparing normal cells.

The ability of TRAIL to selectively induce apoptosis in cancer cells has made it a promising candidate for cancer therapy. Research has shown that TRAIL can effectively target and kill a wide range of tumor cells, including those resistant to conventional therapies. Additionally, TRAIL’s interaction with decoy receptors provides a mechanism to fine-tune its apoptotic activity, potentially reducing off-target effects and enhancing its therapeutic efficacy .