TRAIL is a type II transmembrane protein that can be cleaved to form a soluble protein. The human TRAIL gene is located on chromosome 3q26. The recombinant form of TRAIL, specifically the fragment spanning amino acids 114 to 281, is expressed in Escherichia coli and is often used in research due to its high purity and biological activity .
TRAIL induces apoptosis by binding to its death receptors, DR4 (TRAIL-R1) and DR5 (TRAIL-R2). Upon binding, these receptors undergo trimerization and recruit adaptor proteins such as FADD (Fas-Associated Death Domain), which in turn activate caspase-8. This activation triggers a cascade of downstream caspases, ultimately leading to cell death .
Interestingly, TRAIL can also bind to decoy receptors DcR1 (TRAIL-R3) and DcR2 (TRAIL-R4), which do not induce apoptosis. These decoy receptors can inhibit TRAIL-induced apoptosis by competing with death receptors for TRAIL binding .
TRAIL is unique among the TNF superfamily members due to its ability to selectively induce apoptosis in cancer cells while sparing normal cells. This selective cytotoxicity makes TRAIL a promising candidate for cancer therapy. Studies have shown that recombinant human TRAIL can induce apoptosis in various cancer cell lines, including those resistant to conventional therapies .
Recombinant human TRAIL (114-281 a.a.) is widely used in research to study apoptosis mechanisms and to develop potential cancer therapies. Its high purity and biological activity make it suitable for various applications, including: