Recombinant Human Di-Ub/Ub2 Non-hydrolyzable (K11-linked) CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Di-Ub/Ub2 Non-hydrolyzable (K11-linked) CF Summary

Details of Functionality

Ubiquitin chains vary in length, linkage, and function. K11-linked Non-hydrolyzable Di-Ubiquitin Chains (Ub2) 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 Di-Ubiquitin protein
Each Ubiquitin contains a Pro substitution at position 73.
Accession #
Protein/Peptide Type
Recombinant Proteins
Gene
UBB
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a solution in deionized water.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Reconstitution Instructions
Reconstitute at 5 mg/ml in aqueous buffer.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Di-Ub/Ub2 Non-hydrolyzable (K11-linked) CF

  • DiUbiquitin
  • Di-Ubiquitin
  • Ub2

Background

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 (1). Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse Ubiquitin, respectively (2). 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 (3-8).

Linkage specific, non-hydrolyzable di-Ubiquitin is resistant to the activity of enzymes (DUBs) that cleave the isopeptide 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). Biological roles of K11-linked poly-Ubiquitin are less understood than K48- or K63-linked Ubiquitin chains, though recent evidence points to a role for K11 linkages in the degradation of the anaphase-promoting complex (APC/C), and in TNF-alpha -stimulated NF-kappa B activation.

  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.

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UCN-40
Species: Hu
Applications: Bioactivity

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Bioinformatics

Gene Symbol UBB
Entrez
Uniprot