Goat Anti-Human TNFRSF1A polyclonal antibody for ELISA(Det), WB. TNF receptor 1 (TNF RI; also called TNF R-p55/p60 and TNFRSF1A) is a type I transmembrane protein member of the TNF receptor superfamily member, designated TNFRSF1A. Both TNF RI and TNF RII (TNFRSF1B) are widely expressed and contain four TNF-alpha trimer-binding cysteine-rich domains (CRD) in their extracellular domains (ECD). However, TNF RI is thought to mediate most of the cellular effects of TNF-alpha. It is essential for proper development of lymph node germinal centers and Peyer's patches, and for combating intracellular pathogens such as Listeria. TNF RI is also a receptor for TNF-beta b/TNFSF1B (lymphotoxin-alpha). TNF RI is present on the cell surface as a trimer of 55 kDa subunits. TNF-alpha induces sequestering of TNF RI in lipid rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE. Release of the 28-34 kDa TNF RI ECD also occurs constitutively and in response to products of pathogens such as LPS, CpG DNA or S. aureus protein A. Full-length TNF RI may also be released in exosome-like vesicles. Release helps to resolve inflammatory reactions, since it down-regulates cell surface TNF RI and provides soluble TNF RI to bind TNF-alpha. Exclusion from lipid rafts causes endocytosis of TNF RI complexes and induces apoptosis. Human TNF RI is a 455 amino acid (aa) protein that contains a 21 aa signal sequence, a 190 aa ECD with a PLAD domain that mediates constitutive trimer formation, followed by the four CRD, a 23 aa transmembrane domain, and a 221 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain. The ECD of human TNF RI shows 80%, 80%, 73%, 69% and 70% aa identity with dog, cat, pig, rat and mouse TNF RI, respectively; it shows 23% aa identity with the ECD of TNF RII.
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