TRIADs are novel zinc finger proteins characterized by the presence of Cysteine rich TRIAD domain consisting of DRIL motif flanked by 2 RING fingers. TRIAD3, a 56 kDa protein, is a novel member of this family. It contains 4 RLD domains in the centre and a proline-rich domain at the C-terminus. Localized in the cytoplasm, it interacts with RIP and inhibits TNF and IL1-induced NF-kappaB activation pathways. Reports suggest TRIAD3 acts as an E3-ubiquitin-protein ligase and promotes ubiquitination and degradation of TLR4 and TLR9, thereby regulating TLR signaling. It also interacts with HIV type I Vif protein and interferes in the early events of HIV-1 replication. This gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.
Immunogen
RNF216 antibody was raised against amino acids 350 - 400 of RNF216 (Human).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
IHCWB
RNF216 antibody can be used in ELISA, Western Blot starting at 1:500 - 1:1000, and immunohistochemistry starting at 5 μg/mL.