The FBXL17 antibody is a research tool designed to detect and study the F-box and leucine-rich repeat protein 17 (FBXL17), a member of the F-box protein family. These proteins are critical components of the SCF (SKP1-Cullin-F-box) ubiquitin ligase complexes, which mediate substrate-specific protein ubiquitination and degradation via the proteasome. FBXL17 contains an F-box domain that facilitates interaction with SKP1. linking it to the core SCF machinery, and a C-terminal leucine-rich repeat (LRR) domain implicated in substrate recognition.
Research on FBXL17 remains emerging, but it is hypothesized to regulate diverse cellular processes, including cell cycle progression, signal transduction, and DNA repair, by targeting specific proteins for ubiquitination. Its involvement in cancer biology has drawn attention, with studies suggesting roles in tumor suppression or oncogenesis depending on cellular context. For example, FBXL17 may degrade oncoproteins like TRAIP, influencing genome stability.
The FBXL17 antibody is utilized in techniques such as Western blotting, immunoprecipitation, and immunofluorescence to analyze protein expression, localization, and interactions. Validation includes testing in knockout cell lines or tissues to confirm specificity. Understanding FBXL17's functions could provide insights into diseases linked to ubiquitination dysregulation, including cancers, neurodegenerative disorders, and developmental abnormalities. However, further studies are required to fully elucidate its substrates, regulatory mechanisms, and therapeutic potential.