Anti-TNF Receptor I/TNFRSF1A Antibody Picoband® Fluoro594 Conjugated

Tumor necrosis factor receptor 1 (TNFR1), a potent cytokine, elicits a broad spectrum of biologic responses which are mediated by binding to a cell surface receptor. Its gene is located on 12p13.2. The coding region and the 3-prime untranslated region of TNFR1 are distributed over 10 exons. There are 2 different proteins that serve as major receptors for TNF-alpha, one associated with myeloid cells and one associated with epithelial cells. Additionally, TNFR1 associates with the MADD protein through a death domain-death domain interaction. MADD provides a physical link between TNFR1 and the induction of mitogen-activated protein (MAP) kinase (e.g., ERK2) activation and arachidonic acid release. TNFR1-induced apoptosis involves 2 sequential signaling complexes. Complex I, the initial plasma membrane-bound complex, consists of TNFR1, the adaptor TRADD, the kinase RIP1, and TRAF2 and rapidly signals activation of NF-kappa-B. In a second step, TRADD and RIP1 associate with FADD and caspase-8, forming a cytoplasmic complex, complex II.

Tumor necrosis factor receptor superfamily member 1A; Tumor necrosis factor receptor 1; TNF-R1; Tumor necrosis factor receptor type I; TNF-RI; TNFR-I; p55; p60; CD120a; Tumor necrosis factor receptor superfamily member 1A, membrane form; Tumor necrosis factor-binding protein 1; TBPI; TNFRSF1A; TNFAR, TNFR1

Antiviral Signaling, Apoptosis, Associated Proteins, Cancer, Cell Biology, Cell Death, Growth Factors/Hormones, Immune System Diseases, Immunology, Receptors, Signal Transduction

Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate- specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.

1. Fuchs, P.; Strehl, S.; Dworzak, M.; Himmler, A.; Ambros, P. F. : Structure of the human TNF receptor 1 (p60) gene (TNFR1) and localization to chromosome 12p13. Genomics 13: 219-224, 1992. 2. Hohmann, H.-P.; Remy, R.; Brockhaus, M.; van Loon, A. P. G. M. : Two different cell types have different major receptors for human tumor necrosis factor (TNF-alpha) . J. Biol. Chem. 264: 14927-14934, 1989. 3. Schievella, A. R.; Chen, J. H.; Graham, J. R.; Lin, L.-L. : MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase. J. Biol. Chem. 272: 12069-12075, 1997. 4. Micheau, O.; Tschopp, J. : Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114: 181-190, 2003.

Cell membrane ; Single-pass type I membrane protein . Golgi apparatus membrane ; Single- pass type I membrane protein . Secreted . A secreted form is produced through proteolytic processing.