TRIAD3 Background Information TRIAD protein family members typically contain a double RING finger-linked (DRIL) domain, which consists of 2 RING fingers flanked by a conserved cysteine-rich zinc-binding region, allowing them to interact with several other proteins. TRIAD3 (Triad domain-containing protein 3), also known as E3 ubiquitin-protein ligase RNF216 or Zinc finger protein inhibiting NF-kappa-B (ZIN), is a 866 amino acid cytoplasmic protein that acts as a E3 ubiquitin-protein ligase and enhances ubiquination, and therefore degradation, of TLR4 and TLR9. This evidence suggests that TRIAD3 may regulate the duration and intensity of Toll-like receptor signaling. TRIAD3, which is highly expressed in testis and peripheral blood lymphocytes, also inhibits IL-1 and TNF-induced NF˚B activation pathways and promotes RIP and TNF-mediated apoptosis. There are three isoforms of TRIAD3 that exist as a result of alternative splicing events.
TRIAD3 (D-23)
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TRIAD3 (D-23): sc-130901. Immunoperoxidase staining of formalin-fixed, paraffin-embedded human breast carcinoma tissue showing cytoplasmic localization.
TRIAD3 (D-23): sc-130901. Western blot analysis of TRIAD3 expression in mouse kidney tissue extract.
