DcR1 is found in most normal human tissue, but not in most cancer cell lines. It is a member of the TNF family of TRAIL (TNF-related apoptosis-induced ligand) receptors.
Immunogen
synthetic peptide corresponding to amino acids 111-123 at the extracellular domain of human DcR1 precursor.
Application
Anti-DcR1 antibody produced in rabbit is suitable for immunoblotting at a working concentration of 0.5-1μg/mL using human HeLa cells and mouse and rat liver tissue lysates.
Biochem/physiol Actions
DcR1 is a glycosylphosphatidylinositol-linked membrane protein that binds TRAIL (APO2 ligand). It acts as a decoy receptor and binds TRAIL to its extracellular TRAIL-binding domain, thus inhibiting TRAIL-mediated apoptosis. It does not have an intracellular death domain and, therefore, does not induce apoptosis.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
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Current opinion in immunology, 10(5), 559-563 (1998-10-31)
Apoptosis research is benefiting from bioinformatic approaches to identify new components of the cell death machinery and novel cell death inducers/receptors. Over the past year, knowledge of the system involving TNF-related apoptosis-inducing ligand (TRAIL) and its receptors has increased via
Current biology : CB, 7(12), R750-R753 (1998-02-21)
A cell-death signaling system has been described recently that involves the ligand TRAIL and corresponding TRAIL-specific cell-surface receptors. These include two receptors able to transduce a death signal and, as a previously unsuspected control mechanism, two other receptors able to
Science (New York, N.Y.), 277(5327), 815-818 (1997-08-08)
TRAIL, also called Apo2L, is a cytotoxic protein that induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types. An antagonist decoy receptor (designated as
Science (New York, N.Y.), 277(5327), 818-821 (1997-08-08)
TRAIL (also called Apo2L) belongs to the tumor necrosis factor family, activates rapid apoptosis in tumor cells, and binds to the death-signaling receptor DR4. Two additional TRAIL receptors were identified. The receptor designated death receptor 5 (DR5) contained a cytoplasmic
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