Ubiquitin is a small polypeptide that can be conjugated via its C-terminus to amine groups of lysine residue on target proteins. This conjunction is referred to as monoubiquitylation. Additional ubiquitin moieties can be subsequently conjugated to this initial ubiquitin, utilizing any one of the seven lysine residues on the surface of ubiquitin. The formation of these ubiquitin chains is referred to as polyubiquitylation. This tag-free recombinant form of human ubiquitin is engineered to have a single substitution of arginine for lysine at position 11. Covalent attachment of ubiquitin to other proteins serves various functions, but its major role is to target cellular proteins for destruction. Cellular components that activate, transfer, re