ABCE1 (ATP-binding cassette sub-family E member 1), also known as RNase L inhibitor (RLI), is a conserved eukaryotic protein with dual roles in fundamental cellular processes. It belongs to the ATP-binding cassette (ABC) transporter superfamily but lacks transmembrane domains, distinguishing it from classical ABC transporters. Structurally, ABCE1 contains two nucleotide-binding domains and an iron-sulfur cluster, critical for its ATPase activity. Functionally, it is essential for ribosome biogenesis and translation termination, interacting with release factors to dissociate ribosomes after protein synthesis. Additionally, ABCE1 regulates innate immunity by inhibiting RNase L, an endoribonuclease activated during viral infections to degrade viral and host RNA. This dual role links ABCE1 to viral pathogenesis and interferon-mediated antiviral responses.
ABCE1 antibodies are vital tools for studying its expression, localization, and interactions. They enable detection via techniques like Western blot, immunofluorescence, and immunoprecipitation, aiding research on its roles in cell proliferation, viral defense, and cancer. Dysregulation of ABCE1 has been implicated in tumor progression, HIV replication, and neurodegenerative diseases, making it a potential therapeutic target. Antibodies targeting specific epitopes help dissect its molecular mechanisms and validate its involvement in disease pathways. As ABCE1 is ubiquitously expressed and evolutionarily conserved (from archaea to humans), these antibodies also facilitate cross-species comparative studies. Their applications span virology, oncology, and translational research, underscoring ABCE1's multifaceted biological significance.