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.
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.
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.
Applications:Suitable for use in Western Blot and Immunohistochemistry.