ASB8 (Ankyrin Repeat and SOCS Box Protein 8) is a member of the ASB family, characterized by tandem ankyrin repeats that mediate protein-protein interactions and a C-terminal SOCS box domain involved in ubiquitination pathways. It functions as an adaptor component of E3 ubiquitin ligase complexes, linking substrate recognition (via ankyrin repeats) to the ubiquitin-proteasome system through interactions with Elongin B/C, Cullin5. and RING-box proteins. ASB8 is implicated in diverse cellular processes, including signal transduction, cell cycle regulation, and apoptosis. Studies suggest its role in modulating pathways such as TGF-β signaling, with potential involvement in cancer progression, neuronal development, and metabolic disorders.
ASB8 antibodies are essential tools for detecting ASB8 expression, localization, and protein interactions in research. They enable investigations into its physiological roles and dysregulation in diseases. For example, altered ASB8 levels have been observed in certain tumors, correlating with proliferation or invasion. Commercially available antibodies are typically validated for applications like Western blotting, immunohistochemistry, and co-immunoprecipitation. However, functional studies remain limited, and ASB8's precise molecular mechanisms and disease relevance require further exploration. Its dual-domain structure and regulatory roles position ASB8 as a potential therapeutic target or biomarker in cellular homeostasis and pathology.