Gel-Based Customizable In Vitro E3 Ligase Activity Kit (Alexa647)

Ubiquitin is a small (~8.6 kDa) polypeptide that can be conjugated via its C-terminus to amine groups of lysine residues on target proteins. This conjugation is referred to as monoubiquitylation. Additional ubiquitin moieties can be conjugated to this initial ubiquitin utilizing any one of the seven lysine residues present in ubiquitin. The formation of these ubiquitin chains is referred to as polyubiquitylation. The most well characterized of this polyubiquitylation is chain formation via lysine at position 48 of ubiquitin (K48- linked chains). Monoubiquitylation has been shown to alter the localization, activity, and/or function of the target protein. The most prevalent consequence of polyubiquitylation is the proteasome-mediated degradation of the target protein.