Apoptosis, or programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptosis is induced by certain cytokines including tumor necrosis factor (TNF) and Fas ligand in the TNF family through their death domain containing receptors, TNF receptor 1 (TNFR1) and Fas, respectively. Another member in the TNF family has been identified and designated TRAIL (for TNF-related apoptosis inducing ligand) and Apo-2L (for Apo-2 ligand). Receptors for TRAIL include two death domain containing receptors, DR4 and DR5, as well as two decoy receptors, DcR1 and DcR2, lacking the intracellular signaling death domain.
DcR1 (also called TRID), like the related death receptors DR4 and DR5, contains two extracellular cysteine rich domains. However, DcR1 contains no intracellular death domain and is thus incapable of signaling apoptosis. It has been suggested DcR1 is responsible for TRAIL resistance in normal human tissues including heart, placenta, lung, liver, kidney, spleen, and bone marrow.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 1 µg/ml. Detects a band of approximately 30 kDa (predicted molecular weight: 31 kDa).Can be blocked with DcR1 peptide (ab5849).
Use at an assay dependent concentration.
DcR1 / TRAIL-R3 / TRID / LIT is one of the two putative decoy receptors identified for TRAIL, one of the members of TNF family of apoptosis inducing proteins. The other putative decoy receptor is called DcR2 / TRUNDD / TRAIL-R4. DcR1 is attached to the cell surface through glycophospholipid anchor. It has the extracellular TRAIL binding domain but lacks the cytoplasmic domain to induce apoptotic signal. Hence overexpression of DcR1 inhibits the TRAIL induced apoptosis.