K48-linked Tri-Ubiquitin (human) (rec.) (untagged)

Ub3

Lot dependent.

32160000

liquid

Liquid. In PBS.

Aliquot to avoid freeze/thaw cycles.

Recombinant Protein. Three enzymatically conjugated human ubiquitin (aa1-76) (Accession Nr. P0CG47 http://www.ncbi.nlm.nih.gov/protein/P0CG47 ) covalently linked through an isopeptide bond at K48 residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule and untagged. Produced in E. coli. Liquid. In PBS. The array of cellular processes initiated and regulated by ubiquitin has been partially explained by the structural diversity of differently linked ubiquitin chains. In a ubiquitin chain, ubiquitin moieties can be conjugated through one of their lysine residues (K6, K11, K27, K29, K33, K48 and K63) or the N-terminal methionine residue (M1), offering countless possibilities to assemble a specific polymer. Ubiquitin molecules can also be modified by other post-translational modifications, including acetylation and phosphorylation, adding another layer of ubiquitin signal regulation and diversification. K48-polyubiquitin chains are the most abundant linkage in cells and thought to be the major signal for proteasome-mediated degradation. Quantitative MS analyses of intracellular ubiquitin linkages reveled K48-polyubiquitin linkages rapidly accumulate when cells are treated with the proteasome inhibitor MG132. This protein is formed with wild-type human recombinant ubiquitin and linkage-specific enzymes. Ideal for investigating ubiquitin-binding proteins and as substrates for ubiquitin-specific isopeptidases. Reaction conditions will need to be optimized for each specific application. This K48-linked Triubiquitin is enzymatically conjugated, and purified via liquid chromatography.

P0CG47

Plastic Vial

The array of cellular processes initiated and regulated by ubiquitin has been partially explained by the structural diversity of differently linked ubiquitin chains. In a ubiquitin chain, ubiquitin moieties can be conjugated through one of their lysine residues (K6, K11, K27, K29, K33, K48 and K63) or the N-terminal methionine residue (M1), offering countless possibilities to assemble a specific polymer. Ubiquitin molecules can also be modified by other post-translational modifications, including acetylation and phosphorylation, adding another layer of ubiquitin signal regulation and diversification. K48-polyubiquitin chains are the most abundant linkage in cells and thought to be the major signal for proteasome-mediated degradation. Quantitative MS analyses of intracellular ubiquitin linkages reveled K48-polyubiquitin linkages rapidly accumulate when cells are treated with the proteasome inhibitor MG132. This protein is formed with wild-type human recombinant ubiquitin and linkage-specific enzymes. Ideal for investigating ubiquitin-binding proteins and as substrates for ubiquitin-specific isopeptidases. Reaction conditions will need to be optimized for each specific application. This K48-linked Triubiquitin is enzymatically conjugated, and purified via liquid chromatography.

>98% (SDS-PAGE)

Three enzymatically conjugated human ubiquitin (aa1-76) (Accession Nr. P0CG47 http://www.ncbi.nlm.nih.gov/protein/P0CG47 ) covalently linked through an isopeptide bond at K48 residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule and untagged.

E. coli

no TAG

Non-hazardous

Other Proteins

12352202

Stable for at least 1 year after receipt when stored at -80°C.