Tumor Necrosis Factor Receptors (TNFRs) are a group of receptors that bind to Tumor Necrosis Factors (TNFs), which are cytokines involved in systemic inflammation and are part of the body’s immune response. The TNFR family plays a crucial role in regulating immune cells, apoptosis, and inflammation.
The Tumor Necrosis Factor Receptor Type (Human Recombinant, His Tag) is a recombinant protein produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 161 amino acids, with a molecular weight of approximately 22.68 kDa. This protein is fused with a 4.5 kDa amino-terminal hexahistidine tag (His Tag) to facilitate purification and detection .
The TNFRs are characterized by their ability to bind TNFs via an extracellular cysteine-rich domain. This interaction is crucial for the receptor’s role in mediating the effects of TNFs, which include cell proliferation, differentiation, and apoptosis .
There are two main types of TNFRs:
The recombinant form of TNFR with a His Tag is widely used in research and therapeutic applications. The His Tag allows for easy purification and detection using nickel affinity chromatography and anti-His antibodies, respectively. This makes it a valuable tool for studying the receptor’s function and for developing therapeutic agents targeting TNFRs.
TNFRs, particularly TNFR2, have been identified as potential therapeutic targets for various diseases, including cancer and autoimmune disorders. TNFR2 promotes tumor immune escape by stimulating immune suppressive cell types, such as regulatory T-cells (Tregs) and myeloid-derived suppressor cells (MDSCs). This makes it a promising target for cancer immunotherapy .