With a predicted molecular weight of 26 kDa, tri-Ubiquitin chains are composed of three Ubiquitin monomers that are covalently linked through isopeptide bonds, which typically form between a lysine residue of one Ubiquitin molecule and the C-terminal glycine residue of another Ubiquitin (1). Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa sequence identity with yeast and mouse Ubiquitin, respectively (2). Seven of the 76 aa in Ubiquitin are lysine residues that can participate in poly-Ubiquitin chain formation. Linkage through specific lysine residues is thought to serve as a signal that affects protein degradation, signaling, trafficking, and other cellular processes (3-8).
Linkage specific, non-hydrolyzable tri-Ubiquitin is resistant to the activity of deubiquitinating enzymes (DUB's) that cleave the isopeptide linkage between adjacent Ubiquitin molecules. It can be used to investigate binding interactions between tri-Ubiquitin and proteins that contain elements such as Ubiquitin-associated domains (UBAs) or Ubiquitin-interacting motifs (UIMs). This product may also be useful in exploring the role of unanchored poly-Ubiquitin chains in some signaling pathways.
