Recombinant Human Linear Tetra-Ub Non-hydrolyzable, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human Linear Tetra-Ub Non-hydrolyzable, CF Summary

Details of Functionality
Ubiquitin chains vary in length, linkage, and function. -linked Linear Non-hydrolyzable Tetra-Ubiquitin Chains (Ub4) 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 Tetra-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

Applications/Dilutions

Theoretical MW
34 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

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 2 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 Linear Tetra-Ub Non-hydrolyzable, CF

  • HEL-S-50
  • TetraUbiquitin
  • Tetra-Ubiquitin
  • Ub4
  • UBB
  • ubiquitin B

Background

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 (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). 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).

This linear Ubiquitin fusion protein is resistant to the activity of deubiquitinating enzymes (DUB's) that cleave the peptide linkage between adjacent Ubiquitin molecules.  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 DUB's at the appropriate junction points to yield active Ubiquitin monomers with C-termini ending in GG.  There are likely several intracellular DUB's which perform this essential processing role.  This protein may be useful in analyzing interactions between linear Ubiquitin and proteins that contain Ubiquitin-associated domains (UBA's) or Ubiquitin-interacting motifs (UIM's). 

  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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Bioinformatics

Gene Symbol UBB
Uniprot