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Protein

E. coli

Four human ubiquitin (Accession Nr. P0CG47) covalently linked through isopeptide bonds, including one K63-linkage between two K48-linkages.

Human

Lyophilized.

Use: Formed with wild-type human recombinant ubiquitin and linkage-specific enzymes, which results in one K63-linkage between two K48-linkages. 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-Ubiquitin is the minimal unit necessary for recognition by the 26S proteasome and contains structural characteristic (such as repeating hydrophobic patches) not present in di-ubiquitin. Typical concentrations will depend on specific assay conditions and method of detection.

Manufactured by Boston Biochem

BLUE ICE

+4°C

-20°C

Aliquot to avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -20°C.

No

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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. Each human ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse ubiquitin, respectively. 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.