More Information Product Details
Product Type Protein |
Properties
Source/Host E. coli |
Sequence Four human ubiquitin (Accession Nr. P0CG47) covalently linked through isopeptide bonds at K11 residues of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule. |
Crossreactivity Human |
MW ~34kDa |
Purity ≥95% (SDS-PAGE) |
Concentration 1mg/ml |
Formulation Liquid. In sterile, deionized water. |
Other Product Data Use: Formed with wild-type human recombinant ubiquitin and linkage-specific enzymes. Validated by Ub-AQUA, an LCMS-based technique that provides extremely accurate information on the composition of Poly-ubiquitin samples. Linkage-specific tetra-ubiquitin can be used to investigate mechanism of binding and recognition by E1 or E2 enzymes, deubiquitinating enzymes, E3 ligases or other proteins that contain ubiquitin-associated domains (UBAs) or ubiquitin-interacting motifs (UIMs). Ideal for investigating ubiquitin-binding proteins and as substrates for ubiquitin-specific isopeptidases. 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 |
Declaration Manufactured by Boston Biochem |
Shipping and Handling
Shipping DRY ICE |
Short Term Storage -20°C |
Long Term Storage -80°C |
Handling Advice Avoid freeze/thaw cycles. |
Use/Stability Stable for at least 1 year after receipt when stored at -80°C. |
Documents
MSDS Download PDF |
Product Specification Sheet
Datasheet Download PDF |
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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