Recombinant Human FBXW7 protein

FBXW7 (F-box and WD repeat domain-containing 7) is a critical substrate-recognition component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which regulates protein degradation via the ubiquitin-proteasome system. As a tumor suppressor, FBXW7 targets numerous oncoproteins—including c-MYC, Cyclin E, NOTCH, and mTOR—for ubiquitination and subsequent proteasomal degradation, thereby controlling cell cycle progression, differentiation, and genomic stability. Its dysfunction, caused by mutations or downregulation, is frequently observed in cancers, contributing to oncoprotein accumulation and tumorigenesis.

Recombinant FBXW7 protein is engineered using molecular cloning techniques, typically expressed in *E. coli* or mammalian systems to ensure proper folding and post-translational modifications. This purified protein retains the functional WD40 repeat domain essential for substrate binding and the F-box domain for SKP1 interaction. Researchers employ recombinant FBXW7 to study its biochemical interactions, substrate specificity, and regulatory mechanisms in vitro. It also serves as a tool for high-throughput drug screening to identify compounds that restore FBXW7 activity in cancer models or modulate its degradation pathways.

Additionally, recombinant FBXW7 is utilized in structural studies (e.g., X-ray crystallography or cryo-EM) to elucidate its binding interfaces with substrates or therapeutic molecules. Its applications extend to developing targeted therapies, such as stabilizing FBXW7 or mimicking its function to counteract oncogenic signaling. The production of active, soluble recombinant FBXW7 remains challenging due to its multidomain architecture, necessitating optimization of expression conditions. Nonetheless, it represents a vital reagent for advancing cancer research and precision medicine strategies.