Recombinant Human Ubiquitin Mutant No K Protein, CF

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Recombinant Human Ubiquitin Mutant No K Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Recombinant Human Ubiquitin Mutant No-K can be conjugated to substrate proteins via the subsequent actions of a Ubiquitin-activating (E1) enzyme, a Ubiquitin-conjugating (E2) enzyme, and a Ubiquitin ligase (E3). Recombinant Human Ubiquitin Mutant No-K is unable to form chains, making it ideal for use as a negative control for chain formation or to confirm multi-mono-ubiquitination of a substrate. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human Ubiquitin Mutant No-K concentration of 0.2-1 mM.
E. coli-derived human Ubiquitin protein
Accession #
Predicted Molecular Mass
8.8 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 10 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: Ubiquitin

Ubiquitin is a 76 amino acid (aa) protein that is ubiquitously expressed in all eukaryotic organisms. Ubiquitin is highly conserved with 96% aa sequence identity shared between human and yeast Ubiquitin, and 100% aa sequence identity shared between human and mouse Ubiquitin (1). In mammals, four Ubiquitin genes encode for two Ubiquitin-ribosomal fusion proteins and two poly-Ubiquitin proteins. Cleavage of the Ubiquitin precursors by deubiquitinating enzymes gives rise to identical Ubiquitin monomers each with a predicted molecular weight of 8.6 kDa. Conjugation of Ubiquitin to target proteins involves the formation of an isopeptide bond between the C-terminal glycine residue of Ubiquitin and a lysine residue in the target protein. This process of conjugation, referred to as ubiquitination or ubiquitylation, is a multi-step process that requires three enzymes: a Ubiquitin-activating (E1) enzyme, a Ubiquitin-conjugating (E2) enzyme, and a Ubiquitin ligase (E3). Ubiquitination is classically recognized as a mechanism to target proteins for degradation and as a result, Ubiquitin was originally named ATP-dependent Proteolysis Factor 1 (APF-1) (2,3). In addition to protein degradation, ubiquitination has been shown to mediate a variety of biological processes such as signal transduction, endocytosis, and post-endocytic sorting (4-7).

This Ubiquitin mutant contains no lysine residues, with all lysines mutated to arginine. This mutation renders Ubiquitin unable to form  isopeptide-linked poly-Ubiquitin chains and is useful as a negative control.

  1. Sharp, P.M. & W.-H. Li. (1987) Trends Ecol. Evol. 2:328.
  2. Ciechanover, A. et al. (1980 ) Proc. Natl. Acad. Sci. USA 77:1365.
  3. Hershko, A. et al. (1980) Proc. Natl. Acad. Sci. USA 77:1783.
  4. Greene, W. et al. (2012) PLoS Pathog. 8:e1002703.
  5. Tong, X. et al. (2012) J. Biol. Chem. 287:25280.
  6. Wei, W. et al. (2004) Nature 428:194.
  7. Wertz, I.E. et al. (2004) Nature 430:694.
Entrez Gene IDs
7314 (Human); 298693 (Rat)
Alternate Names
RPS27A; UBA52; UBB ubiquitin B; UBB; UBC; Ubiquitin

Citations for Recombinant Human Ubiquitin Mutant No K Protein, 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.

4 Citations: Showing 1 - 4
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  1. A distinct mammalian disome collision interface harbors K63-linked polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation
    Authors: M Narita, T Denk, Y Matsuo, T Sugiyama, C Kikuguchi, S Ito, N Sato, T Suzuki, S Hashimoto, I Machová, P Tesina, R Beckmann, T Inada
    Nature Communications, 2022;13(1):6411.
    Species: N/
    Sample Types:
  2. CRL4AMBRA1 is a master regulator of D-type cyclins
    Authors: D Simoneschi, G Rona, N Zhou, YT Jeong, S Jiang, G Milletti, AA Arbini, A O'Sullivan, AA Wang, S Nithikasem, S Keegan, Y Siu, V Cianfanell, E Maiani, F Nazio, F Cecconi, F Boccalatte, D Fenyö, DR Jones, L Busino, M Pagano
    Nature, 2021;592(7856):789-793.
    Species: Human
    Sample Types: Peptide
    Applications: Bioassay
  3. The Ubiquitin Ligase CHIP Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover
    Authors: R Tawo, W Pokrzywa, É Kevei, ME Akyuz, V Balaji, S Adrian, J Höhfeld, T Hoppe
    Cell, 2017;169(3):470-482.e13.
    Applications: Bioassay
  4. Ubiquitination and regulation of AURKA identifies a hypoxia-independent E3 ligase activity of VHL
    Authors: E Hasanov, G Chen, P Chowdhury, J Weldon, Z Ding, E Jonasch, S Sen, CL Walker, R Dere
    Oncogene, 2017;0(0):.
    Species: N/A
    Sample Types: Protein
    Applications: Ubiquitination


  1. Is there a N-terminal amino acid sequence modification for the Recombinant Human Ubiquitin Mutant No K Protein, CF (Catalog # UM-NOK)?

    • UM-NOK is the Ubiquitin mutant that contains no lysine residues. However, there is modification of the amino acid sequence (Accession # P0CG47), where all lysines are mutated to arginines, including in the N-terminal sequence. The purpose of this mutation is to make the protein unable to form isopeptide-linked poly-Ubiquitin chains and can be useful as a negative control.

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