SKI antibodies are immunological tools targeting the SKI proto-oncogene protein, a transcriptional regulator implicated in diverse cellular processes. The SKI gene, first identified through its homology to the viral oncogene v-ski, encodes a multifunctional protein that primarily modulates TGF-β and Wnt signaling pathways. SKI binds to SMAD proteins, repressing TGF-β-mediated transcriptional activation and influencing cell proliferation, differentiation, and apoptosis. Its overexpression is linked to oncogenesis, particularly in cancers like melanoma and leukemia, where it promotes tumor progression by inhibiting TGF-β’s tumor-suppressive effects.
SKI antibodies are widely used in research to study SKI’s expression patterns, molecular interactions, and functional roles. They enable techniques such as Western blotting, immunofluorescence, and chromatin immunoprecipitation (ChIP), helping elucidate SKI’s involvement in embryonic development, tissue homeostasis, and cancer. Structurally, SKI contains highly conserved domains, including the SMAD-binding and coiled-coil regions, which are critical for its regulatory functions. Mutations or dysregulation in these domains correlate with developmental disorders and malignancies.
Recent studies highlight SKI’s dual role as both oncogene and tumor suppressor, depending on cellular context and post-translational modifications. Antibodies targeting specific phosphorylation sites or isoforms have advanced understanding of its context-dependent behavior. Additionally, SKI’s interaction with histone deacetylases (HDACs) and chromatin remodeling complexes underscores its epigenetic regulatory potential. Current research focuses on SKI as a therapeutic target, with antibodies aiding in drug discovery and biomarker validation for precision oncology approaches.