Anti-TNFR1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. 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. Protein function: 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. [The UniProt Consortium]