Recombinant Human Tri-Ub Non-hydrolyzable (K48-linked), CF

Catalog # Availability Size / Price Qty
UCN-215-025
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Recombinant Human Tri-Ub Non-hydrolyzable (K48-linked), CF Summary

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Activity
Ubiquitin chains vary in length, linkage, and function. K48-linked Non-hydrolyzable Tri-Ubiquitin Chains (Ub3) may be useful for investigating Ubiquitin-binding proteins and exploring the role of unanchored 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 <40 °C for 20 minutes prior to gel electrophoresis.
Source
E. coli-derived human Tri-Ubiquitin protein

Each Ubiquitin contains a Pro substitution at position 73.

Accession #
Predicted Molecular Mass
26 kDa

Product Datasheets

UCN-215

Formulation Lyophilized from a solution in deionized water.
Reconstitution Reconstitute at 2 mg/ml in an aqueous buffer.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Tri-Ubiquitin

With a predicted molecular weight of 26 kDa, tri-Ubiquitin chains are composed of three 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 (1). Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa sequence identity with yeast and mouse Ubiquitin, respectively (2). 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 (3-8).

Linkage specific, non-hydrolyzable tri-Ubiquitin is resistant to the activity of deubiquitinating enzymes (DUB's) that cleave the isopeptide linkage between adjacent Ubiquitin molecules. It can be used to investigate binding interactions between tri-Ubiquitin and proteins that contain elements such as Ubiquitin-associated domains (UBAs) or Ubiquitin-interacting motifs (UIMs). This product may also be useful in exploring the role of unanchored poly-Ubiquitin chains in some signaling pathways.

 

References
  1. Scheffner, M. et al. (1995) Nature 373:81.
  2. Sharp, P.M. & W.-H. Li (1987) Trends Ecol. Evol. 2:328.
  3. Behrends, C. & J.W. Harper (2011) Nat. Struct. Mol. Biol. 18:520.
  4. Greene, W. et al. (2012) PLoS Pathog. 8:e1002703.
  5. Henry, A.G. et al. (2012) Dev. Cell 23:519.
  6. Tong, X. et al. (2012) J. Biol. Chem. 287:25280.
  7. Wei, W. et al. (2004) Nature 428:194.
  8. Zhang, J. et al. (2012) J. Biol. Chem. 287:28646.
 
Entrez Gene IDs
7314 (Human)
Alternate Names
TriUbiquitin; Tri-Ubiquitin; Ub3

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