Overview
- Peptide CRKNQYRHYWSEN, corresponding to amino acid residues 127-139 of human TNFR1 (Accession P19438). Extracellular, N-terminus
Western blot analysis of human MCF-7 breast adenocarcinoma cell line lysate:1. Anti-Human TNF Receptor I (extracellular) Antibody (#ANT-041), (1:200).
2. Anti-Human TNF Receptor I (extracellular) Antibody, preincubated with Human TNF Receptor I (extracellular) Blocking Peptide (#BLP-NT041).
Western blot analysis of human PANC-1 pancreas ductal adenocarcinoma cell line lysate:1. Anti-Human TNF Receptor I (extracellular) Antibody (#ANT-041), (1:200).
2. Anti-Human TNF Receptor I (extracellular) Antibody, preincubated with Human TNF Receptor I (extracellular) Blocking Peptide (#BLP-NT041).
Cell surface detection of TNFR1 in live intact human MEG-01 megakaryoblastic leukemia cells:___ Cells.
___ Cells + Goat-anti-Rabbit-FITC.
___ Cells + Anti-Human TNF Receptor I (extracellular) Antibody (#ANT-041), 5 µg + Goat-anti-Rabbit-FITC.
- Bradshaw, R.A. and Dennis, E.A. (2009) Handbook of Cell Signaling Volume 1, Second edition.
- Li, J. et al. (2013) Adv. Immunol. 119, 135.
- Sedger, L.M. and Mcdermott, M.F. (2014) Cytokine Growth Factor Rev. 25, 453.
Tumor necrosis factor (TNF) has a wide range of biological effects in host defense against pathogens. It is capable of inducing cell survival, proliferation and differentiation as well as both apoptotic and necrotic cell death under certain conditions. The TNFR1 receptor belongs to a family of type I transmembrane proteins.
TNFR1, as well as other members of its family, is an elongated molecule composed of an extracellular domain of multiple ~40-residue pseudo repeats, with six cysteines forming three disulfide bridges. These modules are termed CRDs (cysteine-rich domains).
Unlike many receptors, TNFR1 does not have enzymatic activity. Instead, an oligomeric complex, called the death domain (DD) places the intracellular regions of the receptor in proximity for recruitment of signaling proteins with enzymatic activities to amplify the signal transduction and mediate extrinsic signal induced cell death1.
TNFα, a ligand of TNFR1 binds to the intracellular death domain of TNFR1 and recruits the TNF receptor-associated DD protein (TRADD), which in turn recruits receptor-interacting protein kinase 1 (RIP1), cellular inhibitor of apoptosis proteins 1 and 2 (cIAP1 and 2), and TNF receptor-associated factor 22.
TNFR1-mediated signaling provides potent anti-viral activity, however many viruses have evolved to encode and express molecules that specifically inhibit almost every step of TNFR-induced apoptosis and NF-κB signaling pathways3.
Anti-Human TNF Receptor I (extracellular) Antibody (#ANT-041) is a highly specific antibody directed against an epitope of the human protein. The antibody can be used in western blot and live cell flow cytometry applications. The antibody recognizes an extracellular epitope and can thus detect the protein in living cells. It has been designed to recognize TNFR1 from human samples only.
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