CUL7 (Cullin 7) is a member of the Cullin protein family, which plays a critical role in the ubiquitin-proteasome system by serving as scaffolds for E3 ubiquitin ligase complexes. Structurally, CUL7 contains a Cullin homology domain, a ROC1-binding domain, and a unique C-terminal region that interacts with adaptor proteins like SKP1 and the F-box protein FBXW8. This assembly facilitates substrate recognition and ubiquitination, targeting specific proteins for degradation. CUL7 is notably involved in cellular processes such as cell cycle regulation, DNA damage response, and cytoskeletal organization.
Mutations in the CUL7 gene are linked to 3M syndrome, a rare genetic disorder characterized by growth retardation, skeletal abnormalities, and facial dysmorphism. Additionally, CUL7 has been implicated in cancer biology. Overexpression of CUL7 is observed in certain malignancies, including breast and lung cancers, where it may promote tumorigenesis by stabilizing oncoproteins or inhibiting tumor suppressors. Conversely, its downregulation has been associated with chemoresistance in some contexts.
CUL7 antibodies are essential tools for studying these biological and pathological mechanisms. They enable the detection of CUL7 expression levels, post-translational modifications, and interactions with binding partners in techniques like Western blotting, immunoprecipitation, and immunohistochemistry. Researchers also use these antibodies to explore CUL7's role in disease models, aiding in the development of targeted therapies for cancers or genetic disorders linked to CUL7 dysfunction.