Negative control for lysine linked polyubiquitination experiments. Recombinant untagged protein.
Contains no lysine residues, with all seven lysines present in the wild type mutated to arginine. These mutations render ubiquitin unable to form multi-ubiquitin chains and thus provide a useful negative control for polyubiquitination experiments. The ability of ubiquitin (no lysine) to form an active thioester at the C-terminus is preserved, thus enabling ubiquitin (no lysine) to be transferred to the lysines of substrate proteins, as is its ability to form linear N-terminal linkages to other ubiquitin molecules. It may also be used as an ubiquitin chain terminator.
