TNFsRI (also known as soluble tumor necrosis factor receptor 1) is a cytokine receptor that binds tumor necrosis factors (TNF). Chan et al. (2000) found that in contrast to the p60 (TNFRSF1A) and p80 (TNFRSF1B; 191191), in the absence of a ligand, TNFA receptors self-assemble through a distinct functional domain in the TNFR extracellular domain, termed the pre-ligand assembly domain (PLAD). Deletion of PLAD results in monomeric presentation of p60 or p80. Flow cytometric analysis showed that efficient TNFA binding depends on receptor self-assembly. They also found that other members of the TNF receptor superfamily, including the extracellular domains of TRAIL (TNFRSF10A; 603611), CD40 (109535), and FAS (TNFRSF6; 134637), all self-associate, but do not interact with heterologous receptors. By Southern blot analysis of human/Chinese hamster somatic cell hybrid DNA, Milatovich et al. (1991) mapped the TNFR1 gene to 12pter-cen. Derre et al. (1991) found by non-radioactive in situ hybridization that the type 1 receptor (the p55 TNF receptor) is encoded by a gene located on chromosome 12p13.2.

ScienCell's human TNFsRI ELISA Kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. Human TNFsRI-specific monoclonal antibodies (clone No. 28401.111) are pre-coated onto 8 x 12 strips. The human-specific detection polyclonal antibodies are biotinylated. The test samples and biotinylated detection antibodies are subsequently added to the wells and then washed with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changes to yellow after adding acidic stop solution. The intensity of yellow is proportional to the amount of human TNFα in the sample that is captured on the strips.

No Publication available at this time