FBXL10 (F-box and leucine-rich repeat protein 10), also known as JHDM1B or KDM2B, is a member of the F-box protein family that plays a role in ubiquitin-mediated proteolysis by forming SCF (Skp1-Cul1-F-box) E3 ubiquitin ligase complexes. It contains an F-box domain for Skp1 binding and leucine-rich repeats (LRRs) for substrate interaction, enabling substrate recognition and degradation. Additionally, FBXL10 functions as a histone demethylase, targeting H3K36me2/me1 through its JmjC domain, thereby regulating gene expression and epigenetic silencing.
FBXL10 antibodies are essential tools for studying its dual role in protein ubiquitination and chromatin remodeling. These antibodies are used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to detect FBXL10 expression, localization, and interactions. Researchers employ them to explore FBXL10's involvement in cellular processes such as cell cycle regulation, differentiation, and tumorigenesis. Studies have linked FBXL10 to both oncogenic and tumor-suppressive activities, depending on cellular context, making it a focus in cancer research.
Antibody specificity is critical due to FBXL10’s splice variants (e.g., FBXL10-1 and FBXL10-2) and post-translational modifications. Validated antibodies help distinguish its roles in recruiting Polycomb repressive complexes or degrading substrates like p53. FBXL10 antibodies also aid in dissecting its tissue-specific functions, particularly in stem cells and developmental models. Overall, these antibodies are vital for unraveling FBXL10's complex regulatory networks in health and disease.