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Protein

E. coli

Four human ubiquitin L73P mutants (Accession Nr. P0CG47) covalently linked through isopeptide bonds at K63 residues of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule.

Human

Lyophilized from a solution in deionized water.

Use: Linkage-specific, non-hydrolyzable tetra-ubiquitin is resistant to the activity of deubiquitinating enzymes (DUBs) that cleave the isopeptide linkage between adjacent ubiquitin molecules. May be useful for investigating ubiquitin-binding and CARD-domain containing proteins and exploring the role of unanchored (free C-terminus) ubiquitin chains in signaling pathways. Reaction conditions will need to be optimized for each specific application. IMPORTANT: Heating this product in SDS-PAGE buffer or terminating reactions containing this product with heated SDS-PAGE buffer could lead to unexpected, high apparent molecular weight banding or smearing on gels that is not representative of product purity. For optimal results, we recommend incubation in SDS-PAGE buffer + DTT at

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.

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