TRAF1 Human

TRAF1 is unique among the TRAF family members as it lacks the RING finger domain, which is typically involved in ubiquitin ligase activity. Despite this, TRAF1 can still interact with other TRAF proteins and TNFR-associated factors to mediate signal transduction. It primarily functions as an adaptor protein, facilitating the assembly of signaling complexes that activate downstream pathways such as NF-κB and MAPK .

TRAF1 is involved in the regulation of immune responses by modulating the signaling pathways initiated by TNF receptors. It plays a significant role in the activation of NF-κB, a transcription factor that controls the expression of various genes involved in immune and inflammatory responses . Additionally, TRAF1 is implicated in the regulation of apoptosis, a process of programmed cell death essential for maintaining tissue homeostasis and immune system function .

Alterations in TRAF1 expression and function have been associated with various diseases, including autoimmune disorders and cancers. For instance, increased levels of TRAF1 have been observed in patients with rheumatoid arthritis, suggesting its involvement in the pathogenesis of this autoimmune disease . Moreover, TRAF1 has been identified as a potential therapeutic target for the treatment of inflammatory and autoimmune diseases due to its role in modulating TNF receptor signaling .

Human recombinant TRAF1 is a bioengineered form of the protein produced using recombinant DNA technology. This involves inserting the TRAF1 gene into an expression vector, which is then introduced into a host cell (such as E. coli or mammalian cells) to produce the protein. Recombinant TRAF1 is used in research to study its structure, function, and interactions with other proteins. It is also utilized in the development of therapeutic agents targeting TNF receptor signaling pathways .