Recombinant Human FBXL2 protein

FBXL2 (F-box and leucine-rich repeat protein 2) is a member of the F-box protein family, which functions as a substrate-recognition component of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. This complex plays a central role in the ubiquitin-proteasome system, targeting specific proteins for degradation through polyubiquitination. Structurally, FBXL2 contains an F-box domain that mediates interaction with Skp1. linking it to the core SCF machinery, and a leucine-rich repeat (LRR) domain involved in substrate binding. Its activity is tightly regulated by post-translational modifications, including phosphorylation, which influences substrate specificity and subcellular localization.

FBXL2 is implicated in diverse cellular processes, such as cell cycle regulation, apoptosis, and immune responses. It selectively targets proteins like the inhibitor of nuclear factor kappa-B (IκB), cyclin D2. and TRAF proteins for degradation, thereby modulating pathways such as NF-κB signaling and inflammation. Studies highlight its role in stress adaptation, where it promotes the turnover of misfolded proteins under proteotoxic conditions. Dysregulation of FBXL2 has been associated with diseases, including cancers (e.g., lung, liver) and neurodegenerative disorders, where altered ubiquitination contributes to pathological protein accumulation or unchecked cell proliferation.

Recombinant FBXL2 protein is engineered for in vitro studies to analyze its biochemical properties, substrate interactions, and regulatory mechanisms. Researchers utilize it to screen small-molecule modulators or dissect SCF complex dynamics, offering insights into therapeutic strategies targeting ubiquitination pathways. Its recombinant form often includes tags (e.g., GST, His) for purification and detection, enabling functional assays that advance understanding of protein homeostasis and disease mechanisms linked to ubiquitin-mediated degradation.