CYTH1 (Cytohesin-1), also known as ARNO (ADP-ribosylation factor nucleotide-binding site opener), is a member of the cytohesin family of guanine nucleotide exchange factors (GEFs). It primarily activates small GTPases of the ADP-ribosylation factor (ARF) family by promoting the exchange of GDP for GTP, a critical step in regulating membrane trafficking, cytoskeletal reorganization, and signal transduction. CYTH1 contains a central Sec7 domain responsible for GEF activity, a pleckstrin homology (PH) domain for membrane targeting, and a coiled-coil domain mediating protein-protein interactions. It plays roles in cellular processes such as cell migration, adhesion, and receptor signaling (e.g., EGFR, insulin receptor).
CYTH1 antibodies are essential tools for studying its expression, localization, and function in various biological contexts. These antibodies are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to detect CYTH1 in cell lines, tissues, or disease models. Research has linked CYTH1 to cancer progression, immune regulation, and metabolic disorders, with studies showing its overexpression in certain cancers (e.g., breast, lung) and involvement in T-cell activation. Antibodies targeting specific epitopes or post-translational modifications of CYTH1 help dissect its regulatory mechanisms and therapeutic potential. Commercial CYTH1 antibodies are typically validated for specificity using knockout controls or siRNA knockdown, ensuring reliability in experimental settings.