With a predicted molecular weight of 17 kDa, Di-Ubiquitin is composed of two Ubiquitin monomers that are covalently linked through an isopeptide bond, which typically form between a lysine residue of one Ubiquitin molecule and the C-terminal glycine residue of another Ubiquitin molecule (1). Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse Ubiquitin, respectively (2). Ubiquitin has seven lysine residues that can participate in the formation of poly-Ubiquitin chains. The specific lysine residue used in Ubiquitin conjugation is thought to determine the function of poly-ubiquitination in cellular processes such as protein degradation, signaling, and trafficking (3-8).
Linkage specific, non-hydrolyzable di-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 di-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.
