The ABCF1 antibody targets the ATP-binding cassette subfamily F member 1 (ABCF1), a ubiquitously expressed protein belonging to the ABC transporter superfamily. Unlike canonical ABC transporters, ABCF1 lacks transmembrane domains, suggesting non-canonical roles in cellular processes. It is implicated in translational regulation, ribosome homeostasis, and immune response modulation. Structurally, ABCF1 contains two nucleotide-binding domains (NBDs) critical for ATP hydrolysis, though its exact molecular mechanisms remain under investigation.
ABCF1 is linked to innate immunity, particularly in regulating inflammatory signaling pathways like NF-κB and interferon responses. Studies highlight its interaction with viral RNAs or host stress granules, positioning it as a mediator of antiviral defenses. Dysregulation of ABCF1 has been associated with autoimmune disorders (e.g., rheumatoid arthritis) and cancers, where its overexpression may influence drug resistance or tumor progression.
Antibodies against ABCF1 are widely used in research to detect protein expression via Western blotting, immunofluorescence, or immunohistochemistry. They also facilitate functional studies, such as exploring ABCF1's role in ribosome-associated quality control or immune signaling cascades. Commercial antibodies are often validated for specificity across human, mouse, and rat models, with epitopes typically targeting conserved regions of the N-terminal or NBD domains. Recent applications include investigating ABCF1 as a potential biomarker in autoimmune diagnostics or as a therapeutic target in oncology.