Tumor necrosis factor-alpha (TNF-α) is a type II transmembrane protein. It exists in membrane-bound form (mTNF-α). mTNF-α can be processed into 17 kDa soluble TNF-α (sTNF-α) through the action of an enzyme called TNFα-converting enzyme.TNF-α functions through two TNF receptor superfamily members, type I transmembrane receptor TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). The extracellular domains of both receptors contain similar cysteine-rich motifs, repeated two to six times. TNFR2 (Tumor Necrosis Factor Receptor 2) is mainly activated by mTNF-α and is predominantly expressed in thymic lymphocytes, endothelial cells, microglial cells, and oligodendroglial cells.When TNF-α binds to TNFR2, the intracellular domain recruits existing cytoplasmic TRAF2-cLAP1-cLAP2 complex, activating downstream signaling pathways. Research has shown that TNFR2 inhibitors can specifically inhibit the proliferation of Treg cells expressing high levels of TNFR2 in the tumor microenvironment, while also selectively killing tumor cells. TNFR2 Reporter V2 Cell Line is a cell line with knockout of the TNFR1 Luciferase reporter gene. Binding of mTNF-α to TNFR2 activates downstream pathways; addition of antagonists blocks the downstream signaling pathway, leading to changes in luciferase expression. Luciferase readings represent the activation effect of the signaling pathway and can be used for in vitro evaluation of TNFR2 antagonists.
