Human TNFR1 Protein, ECD (Extracellular Domain), Fc-fusion, Recombinant

Description :
TNFR1 and TNFR2 are single-pass, type I transmembrane glycoproteins that are two distinct types of high­affinity cell surface receptors for TNF. Both receptors are the founding members of the TNF receptor superfamily (TNFRSF) and are designated TNFRSF1A and TNFRSF1B, respectively. The extracellular regions of both receptors contain 4 conserved cysteine­rich repeats that mediate the interaction with TNF. However their intracellular sequences have no homology, indicative of distinct signaling pathways. TNFR1 and TNFR2 form a heterocomplex on the cell surface that mediates the recruitment of adaptor proteins for signal transduction. Soluble truncated forms of TNFR1 and TNFR2 have been identified in human serum and urine, which can neutralize the biological activities of TNF. Whereas all cell types studied express TNFR1, TNFR2 expression is limited primarily to hematopoietic cells and cells of the immune system. Most of the biological functions of TNF are mediated via TNFR1. TNFR1 can activate NF-κB, mediate apoptosis, and function as a regulator of inflammation. In the cytoplasmic region, TNFR1 contains a neutral sphingomyelinase activation domain and a death domain. TNFR1 is essential for proper development of lymph node germinal centers and Peyer’s patches, and for combating intracellular pathogens such as Listeria. Mutations in the TNFR1 gene are associated with the autosomal dominant periodic familial hibernian fever (FHF) and multiple sclerosis 5 (MS5).