Cul7 Antibody

Cullins assemble a potentially large number of ubiquitin ligases by binding to the RING protein ROC1 to catalyse polyubiquitination, as well as binding to various specificity factors to recruit substrates. Cullin 7 is a component of E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Cullin 7 seems to be involved proteosomal degradation of proteins involved in endothelial proliferation and/or differentiation. Cullin 7 is part of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN isoform 1. Cullin 7 interacts with a complex of SKP1 and FBXW8, but not with SKP1 alone. Anti-Cul7 has been tested by immunohistochemistry. This antibody reacts with human and mouse Cul7 by western blot and immunoprecipitation. The antibody immunoprecipitates in vitro translated protein and also immunoprecipitates protein from cell lysates (using HeLa, NIH-3T3, and others) . This antibody also co-immunoprecipitates associated proteins in overexpressed CUL7 systems. A 191.2 kDa band corresponding to human Cul7 is detected. Most cell lines expressing Cul7 can be used as a positive control. Researchers should determine optimal titers for other applications.