Polyclonal Antibody to DcR1 (TRAIL-R3, TRID, LIT)

Background
Cells undergo programmed cell death (Apoptosis) in response to various stimuli. Apoptosis is essential for morphogenesis, tissue homeostasis, and host defense. Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors, TNFR1 and Fas. A novel death domain containing receptors have been recently identified and designated DR4 and DR5 (for death receptor 4). DR4 and DR5 are functional receptors for TRAIL, and DcR1/TRID and DcR2 are decoy receptors1-3. DcR1 is also designated as TRAIL-R3, TRID or LIT2-7. DcR1 has an extracellular TRAIL-binding domain but lacks intracellular death domain and does not induce apoptosis. TRAIL-R3 also has several sites for potential N- (5 sites) and O-linked (approximately 20) glycosylation and GPI addition. Antibodies made against TRAIL-R3/DcR1 detects a protein of approximate molecular mass of 65kDa in the western blot analysis under denaturing and reducing conditions instead of theoretical Mr of 29 kDa6. The slow migration of this protein in SDS-PAGE is probably due to the presence of 5 TAPE (threonine, alanine, proline, and glutamine-rich) repeats. The TAPE repeat-deficient receptor migrates normally in SDS-PAGE6. Unlike TRAIL-R1 (DR4) and TRAIL-R2 (DR5), DcR1/TRAIL-R3 transcript is restricted to skeletal muscle, peripheral blood lymphocytes, and the spleen.

Antigen
This antibody was raised by immunizing rabbits with a peptide corresponding to aa 149-167 at the extracellular domain of human DcR1 precursor (4-6).

Application Notes
A 65 kDa band is observed.

Genebank Info (Protein)
NP_803187

Reference
1. Sheridan JP, Marsters SA, Pitti RM, Gurney A, Skubatch M, Baldwin D, Ramakrishnan L, Gray CL, Baker K, Wood WI, Goddard AD, Godowski P, Ashkenazi A. Science 1997; 277:818-821.
2. Pan G, O’Rourke K, Chinnaiyan AM, Gentz R, Ebner R, Ni J, Dixit VM. Science 1997;276:111-113.
3. Pan G, Ni J, Wei YF, Yu G, Gentz R, Dixit VM. Science 1997;277:815-818.
4. Degli-Esposti MA, Smolak PJ, Walczak H. et al. J Exp Med 166: 1165-1170 (1997).
5.  McFarlne M, Ahamad M, srinivasan SM et al. J. Biol. Chem 272: 25417-25420 (1997).
6. Shneider P, Bodmer JL, Thome M, Hofmann K, Holler N, and Tschopp J. FEBS Lett. 416: 329-334 (1997).
7. Mongkolsapaya J, Cowper AE, Xu XN, et al. J Immunol 160: 3-6 (1998).