Recombinant Human Tetra-Ub WT Chains (K48-linked) Biotin, CF

Discontinued Product

UCB-210 has been discontinued.
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Recombinant Human Tetra-Ub WT Chains (K48-linked) Biotin, CF Summary

Product Specifications

>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Ubiquitin chains vary in length, linkage, and function. K48-linked Biotinylated Tetra-Ubiquitin Chains (Ub4) are ideal for use in assays that utilize avidin-linked reagents for visualization or quantitation. 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.
E. coli-derived human Tetra-Ubiquitin protein
Accession #
Predicted Molecular Mass
34 kDa

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a solution in deionized water.
Reconstitution Reconstitute at 2 mg/mL in an aqueous solution.
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.
  • 12 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: Tetra-Ubiquitin

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).

Linkage specific Tetra-Ubiquitin can also 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 or Ubiquitin-interacting motifs (UIMs).  This product is formed with wild-type Ubiquitin and linkage-specific enzymes.  Tetra-Ubiquitin is the minimal unit necessary for recognition by the 26S proteasome and contains structural characteristic (such as repeating hydrophobic patches) not present in di-Ubiquitin.  This product is made with wild-type human recombinant Ubiquitin and linkage-specific enzymes. These chains are modified with biotin via primary amine coupling.  This results in multiple biotinylated species modified at the N-terminus, as well as lysine residues.  Biotinylated Ubiquitin can be detected using avidin-linked reagents. 


  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.
  9. Beal R.E., et al. (1995) Biochem. 37:2925-2934.
  10. Cook W. J., et al. (1992) J. Biol. Chem. 267:16467-16471.
  11. Cook W. J. et al. (1994) J. Mol. Biol. 236:601-609.
  12. Phillips C. L., et al. (2001) Acta. Cryst. 57:341-344.
  13. Piotrowski J. et al. (1997) J. Biol. Chem. 272:23712-23721.
  14. Tenno T., et al. (2004) Genes to Cells. 9:865-875.
  15. Wilkinson K.D., et al. (1995) Biochem. 34:14535-14546.
Entrez Gene IDs
7314 (Human)
Alternate Names
HEL-S-50; TetraUbiquitin; Tetra-Ubiquitin; Ub4; UBB; ubiquitin B

Citation for Recombinant Human Tetra-Ub WT Chains (K48-linked) Biotin, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Generation and Validation of Intracellular Ubiquitin Variant Inhibitors for USP7 and USP10
    Authors: W Zhang, MA Sartori, T Makhnevych, KE Federowicz, X Dong, L Liu, S Nim, A Dong, J Yang, Y Li, D Haddad, A Ernst, D Heerding, Y Tong, J Moffat, SS Sidhu
    J. Mol. Biol., 2017;0(0):.
    Applications: Bioassay


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