Collection: TNF Receptor Superfamily Proteins

In human, 29 members of the TNF receptor (TNFR) family have been identified. Most of them are type I membrane proteins with a few exceptions. BCMA, BAFFR, TACI and XEDAR all lack the signal peptide and are classified as type III membrane proteins. Both OPG and DcR3 are soluble proteins and the TRAIL-R3 is tethered to membrane with a glycolipid. In addition, a number of TNFRs including CD27, CD30, CD40, TNFR1 and TNFR2 can be proteolytic processed into soluble receptors. FAS and 4-1BB also express as soluble form by alternatively slicing off the transmenbrane-encoding exon. Soluble receptors, each being able to interact with its ligand, are shown to modulate the activity of the respective membrane anchored receptor. Many TNF receptors interact with more than one ligand. These include both TNFR1 and TNFR2 interact with TNF-α and LT-α, both BCMA and TACI interact with BAFF and APRIL, HVEM interacts with LIGHT, LT-α and BTLA, LTβR interacts with LT-α1β2 and LIGHT, and OPG interact with RANKL and TRAIL. Yet ligands for RELT, TRAMP, TROY and DR6 have not been identified. Almost all ligands for TNFR superfamily members belong to TNF superfamily (TNFSF). The exceptions are HVEM and EGFR as BTLA and NGF/BDNF/neurotropins are structurally unrelated to TNFSF proteins. The increasingly revealed details of the molecular interaction and signaling pathways have made many TNFRSF members targets of vigorous investigations for disease intervention.

Our TNFRSF-Fc fusion proteins are homodimers linked by a pair of disulfide bonds at the hinge region of mouse IgG2a, affinity purified and size-excluded to homogeneity.