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Protein

E. coli

Two human ubiquitin L73P mutants (Accession Nr. P0CG47) covalently linked through an isopeptide bond at K63 residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule, and coupled to agarose.

Human

Agarose

Liquid. Resin supplied as a 50% slurry in 20% ethanol.

Use: Linkage-specific, non-hydrolyzable di-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 proteins and exploring the role of unanchored (free C-terminus) ubiquitin chains in signaling pathways. We recommend to prepare resin by rinsing with 10 volumes of water to remove ethanol storage buffer and equilibrating the resin by washing with 10 volumes of your desired aqueous buffer.Polyubiquitin-agarose can be re-used if properly maintained. After use, clean resin with a wash cycle of 5 volumes 100 mM HEPES pH 8.0, 500mM NaCl followed by 5 volumes 100mM NaOAc pH4.5, 500mM NaCl. Repeat twice, then rinse resin with a low salt buffer.

Manufactured by Boston Biochem

BLUE ICE

+4°C

+4°C

Do not freeze.

Stable for at least 3 months after receipt when stored at +4°C.

No

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