Adipogen/Tetra-ubiquitin [Ub4] Non-hydrolyzable (linear) (human) (rec.) (Agarose)/AG-40T-0395-R250/2

来自 : 发布时间：2025-01-08

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Protein

E. coli

Four human ubiquitin L73P mutants (Accession Nr. P0CG47) covalently linked through the N-terminal amino group of methionine on one ubiquitin that is conjugated with the C-terminal carboxy group of another ubiquitin, and coupled to agarose.

Human

Agarose

Liquid. In 20% Ethanol.

Use: This linear ubiquitin fusion protein is resistant to the activity of deubiquitinating enzymes (DUBs) that cleave the peptide 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) and exploring the role of unanchored (free C-terminus) ubiquitin chains in signaling pathways. Useful for the enrichment of known ubiquitin chain-interacting proteins as well as the discovery of novel ubiquitin chain-interacting proteins. We recommend equilibrating the resin by washing with 10 volumes of your desired aqueous buffer.Storage: 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, 500 mM NaCl followed by5 volumes 100 mM NaOAc pH 4.5, 500 mM NaCl. Repeat twice, then rinse resin with a low salt buffer. Store resin at 4°C in neutral aqueous buffer containing 1 mM NaN3 or 20 % ethanol as a preservative.

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 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. Ubiquitin is not expressed directly as free ubiquitin, but rather as linear fusions either to itself or to certain ribosomal protein subunits. These ubiquitin-fusion precursors are proteolyzed by DUBs at the appropriate junction points to yield active ubiquitin monomers with C-termini ending in GG. There are likely several intracellular DUBs which perform this essential processing role.