Recombinant RN115 protein (His tag)

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Recombinant Human E3 ubiquitin-protein ligase RNF115 fragment (residues 185-272) is a high-purity, stable protein designed for structural and biochemical studies. This 88-amino acid fragment, derived from the full-length RNF115 (EC 2.3.2.27), offers researchers a soluble unit to investigate the mechanisms of ubiquitination, autophagy, and innate immune signaling without the complexities of the full protein.

E3 ubiquitin-protein ligase RNF115 is a multifunctional enzyme that catalyzes Lys-48- and Lys-63-linked polyubiquitination, playing pivotal roles in autophagy, innate immunity, cell proliferation, and endosomal trafficking. It regulates the degradation of receptors such as EGFR and FLT3, supports antiviral responses by targeting HIV-1 virions and retroviral GAG proteins, and modulates innate immunity through ubiquitination of MAVS and STING1. Additionally, RNF115 enhances autophagosome-lysosome fusion by stabilizing STX17 and inhibits TLR-induced inflammation via Rab1A and Rab13 ubiquitination. Located in the cytoplasm, nucleus, endoplasmic reticulum, and Golgi apparatus, it is recruited to late endosomes/lysosomes by GTP-bound RAB7A, underscoring its broad impact on cellular signaling pathways.