DR3, also known as APO-3, TRAMP, LARD, and WSL-1, is a member of the tumor necrosis factor receptor superfamily (TNFRSF) with a typical death domain that consists of an approximately 60-amino-acid globular bundle of 6 conserved α helices found in the cytoplasmic region.
Read all details below including Quick Specs.
** Please note: For orders over 1 mg, please inquire here
|Synonym:||TNFRSF25, APO-3, DDR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR|
|Tag:||Mouse IgG2a Fc|
|Construction:||Human DR3 (A24-Q199)-Mouse IgG2a Fc|
|MW (calculated):||46,194 daltons|
|MW (SDS-PAGE):||50 Kd|
|Abs 0.1% (= 1 mg/ml):||1.202|
DR3, also known as APO-3, TRAMP, LARD, and WSL-1, is a member of the tumor necrosis factor receptor superfamily (TNFRSF) with a typical death domain that consists of an approximately 60-amino-acid globular bundle of 6 conserved α helices found in the cytoplasmic region. Although DR3 is most homologous to TNFR1, which is widely expressed, its expression is mostly restricted to lymphocytes such as NK cells and T cells, in particular NKT cells and is enhanced upon their activation.
DR3 is more highly expressed on Th17 cells than on Th1 and Th2 cells, and is also expressed on naturally occurring and TGF-β-induced Treg cells (n-Treg and i-Treg, resp.). It was recently shown that DR3 expression on B cells was induced by anti-IgM stimulation, although its expression was not detectable on resting B cells. There are several expression differences between human and mouse. DR3 splicing variants of 13 in human and 3 in mice have been identified. Pappu et al. showed that DR3 splicing variants are differentially expressed on T-cell subsets in mice.
There is only one ligand for DR3, TL1A, yet, TL1A also binds to a decoy protein, DcR3. TL1A-DR3 interaction forms a part of the inflammatory cytokine network and contribute to rheumatoid arthritis (RA) and intestinal bowl disease (IBS). The DcR3 functions as a decoy receptor for TL1A as well as FasL and LIGHT.
Amino Acid Sequence.
1. Bull MJ, Williams AS, Mecklenburgh Z, Calder CJ, Twohig JP, et al. (2008) The Death Receptor 3-TNF-like protein 1A pathway drives adverse bone pathology in inflammatory arthritis. J Exp Med. 205:2457-2464.
2. Screaton GR, Xu XN, Olsen AL, Cowper AE, Tan R, McMichael AJ, et al. (1997) LARD: a new lymphoid-specific death domain containing receptor regulated by alternative pre-mRNA splicing. Proc Natl Acad Sci U S A. 94:4615-4619.
3. Tan KB, Harrop J, Reddy M, Young P, Terrett J, Emery J, et al. (1997) Characterization of a novel TNF-like ligand and recently described TNF ligand and TNF receptor superfamily genes and their constitutive and inducible expression in hematopoietic and non-hematopoietic cells. Gene. 204:35-46.
4. Pappu BP, Borodovsky A, Zheng TS, Yang X, Wu P, Dong X, et al. (2008) TL1A-DR3 interaction regulates Th17 cell function and Th17-mediated autoimmune disease. J Exp Med. 205:1049-1062.