RNF11 (Ring Finger Protein 11) is an E3 ubiquitin ligase adaptor protein involved in regulating ubiquitination-mediated protein degradation, a critical process for cellular homeostasis. It modulates key signaling pathways, including TGF-β, NF-κB, and EGFR, by interacting with E3 ligases like SMURF1/2. NEDD4. and Itch to target substrates for proteasomal or lysosomal degradation. Structurally, RNF11 contains a conserved RING-H2 domain, a PY motif, and a TM domain, enabling its role in trafficking and substrate recognition. Dysregulation of RNF11 is linked to cancer progression, neurodegenerative diseases (e.g., Parkinson’s), and immune disorders, highlighting its dual tumor-suppressive or oncogenic roles depending on cellular context.
RNF11 antibodies are essential tools for studying its expression, localization, and molecular interactions. They are widely used in techniques such as Western blotting, immunoprecipitation, and immunohistochemistry to explore RNF11’s regulatory mechanisms in disease models. For instance, these antibodies help identify RNF11’s role in degrading tumor suppressors (e.g., PML) or oncoproteins, as well as its involvement in inflammatory responses via NF-κB inhibition. Commercial RNF11 antibodies are typically validated for specificity against its unique epitopes, though cross-reactivity with homologous proteins (e.g., RNF12) requires careful controls. Research utilizing these antibodies continues to clarify RNF11’s therapeutic potential as a modulator of protein stability pathways.