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.
RNF216 antibody can be used in ELISA, Western Blot starting at 1:500 - 1:1000, and immunohistochemistry starting at 5 ?g/mL.
Protein G Column
PBS, 0.2% gelatin, 0.05% sodium azide.
Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.
Type: Primary
Antigen: RNF216
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human
