TNFRSF13B is a transmembrane protein that interacts with calcium-modulator and cyclophilin ligand (CAML). It plays a significant role in the activation of transcription factors such as NFAT, AP1, and NF-kappa-B. These transcription factors are essential for the regulation of humoral immunity, which involves the production of antibodies by B cells .
The receptor binds to two ligands with high affinity: TNFSF13/APRIL and TNFSF13B/BAFF/BLYS. These interactions are crucial for the stimulation of B- and T-cell functions, as well as the regulation of humoral immunity .
The recombinant form of TNFRSF13B, tagged with a polyhistidine (His) tag, is produced using recombinant DNA technology. The His tag is a sequence of histidine residues added to the protein to facilitate its purification and detection. This tag allows for the efficient isolation of the protein using metal affinity chromatography, which is a common technique in protein purification .
Mutations in the TNFRSF13B gene have been associated with various immunodeficiency disorders, including Common Variable Immunodeficiency (CVID) and Selective IgA Deficiency (IGAD). These conditions are characterized by a reduced ability to produce antibodies, leading to increased susceptibility to infections .
The receptor’s role in immune regulation makes it a potential target for therapeutic interventions in autoimmune diseases and other conditions involving dysregulated immune responses .