With a predicted molecular weight of 34 kDa, Tetra-Ubiquitin chains are composed of four 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 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). 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).
Tetra-Ub can be used to investigate mechanisms of binding and recognition by deubiquitinating enzymes, E3 ligases or other proteins that contain Ubiquitin-associated domains (UBAs) or Ubiquitin-interacting motifs (UIMs). Tetra-Ub is the minimal unit necessary for recognition by the 26S Proteasome and contains structural characteristic (such as repeating hydrophobic patches) not present in di-Ub. This product is made with wild-type human recombinant Ubiquitin and linkage-specific enzymes, which results in one K48-linkage between two K63-linkages.
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