Recombinant Human Ubiquitin Rhodamine 110 Protein, CF

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Product Details
Citations (8)
Reviews (2)

Recombinant Human Ubiquitin Rhodamine 110 Protein, CF Summary

>95%, by HPLC.
Recombinant Human Ubiquitin-Rhodamine110 (R110) is ideal for use in assays requiring fluorescent detection. Optimal fluorescence at pH 8.0 is monitored with an excitation wavelength of 485 nM and an emission wavelength of 535 nM. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human Ubiquitin-Rhodamine110 (R110) concentration of 0.1-1 μM.
E. coli-derived human Ubiquitin protein
Contains a C-terminal Rhodamine 110 (R110)
Accession #
Predicted Molecular Mass
8.9 kDa

Product Datasheets

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 2.23 mg/ml (250 μM) in DMSO
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
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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 fluorogenic substrate is based on the C-terminus derivatization of Ubiquitin with Rhodamine 110 (R110) (8). Similar to Ubiquitin-AMC, this is an exquisitely sensitive deubiquitinating enzyme substrate and is useful for studying Ubiquitin C-terminal hydrolytic activity when detection sensitivity or continuous monitoring is essential.

  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.
  8. Hassiepen, U. et al. (2007) Anal. Biochem. 371: 201.
Entrez Gene IDs
7314 (Human); 298693 (Rat)
Alternate Names
RPS27A; UBA52; UBB ubiquitin B; UBB; UBC; Ubiquitin

Citations for Recombinant Human Ubiquitin Rhodamine 110 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.

8 Citations: Showing 1 - 8
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  1. Hypoxia-induced 26S proteasome dysfunction increases immunogenicity of mesenchymal stem cells
    Authors: E Abu-El-Rub, GL Sequiera, N Sareen, W Yan, M Moudgil, MG Sabbir, S Dhingra
    Cell Death Dis, 2019;10(2):90.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Cytotoxic unsaturated electrophilic compounds commonly target the ubiquitin proteasome system
    Authors: K Selvaraju, A Mofers, P Pellegrini, J Salomonsso, A Ahlner, V Morad, EK Hillert, B Espinosa, ESJ Arnér, L Jensen, J Malmström, MV Turkina, P D'Arcy, MA Walters, M Sunnerhage, S Linder
    Sci Rep, 2019;9(1):9841.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  3. Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
    Authors: DS Hewings, J Heideker, TP Ma, AP AhYoung, F El Oualid, A Amore, GT Costakes, D Kirchhofer, B Brasher, T Pillow, N Popovych, T Maurer, C Schwerdtfe, WF Forrest, K Yu, J Flygare, M Bogyo, IE Wertz
    Nat Commun, 2018;9(1):1162.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  4. ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability
    Authors: P Haahr, N Borgermann, X Guo, D Typas, D Achuthanku, S Hoffmann, R Shearer, TK Sixma, N Mailand
    Mol. Cell, 2018;0(0):.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  5. 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
  6. Molecular basis of USP7 inhibition by selective small-molecule inhibitors
    Authors: AP Turnbull, S Ioannidis, WW Krajewski, A Pinto-Fern, C Heride, ACL Martin, LM Tonkin, EC Townsend, SM Buker, DR Lancia, JA Caravella, AV Toms, TM Charlton, J Lahdenrant, E Wilker, BC Follows, NJ Evans, L Stead, C Alli, VV Zarayskiy, AC Talbot, AJ Buckmelter, M Wang, CL McKinnon, F Saab, JF McGouran, H Century, M Gersch, MS Pittman, CG Marshall, TM Raynham, M Simcox, LMD Stewart, SB McLoughlin, JA Escobedo, KW Bair, CJ Dinsmore, TR Hammonds, S Kim, S Urbé, MJ Clague, BM Kessler, D Komander
    Nature, 2017;550(7677):481-486.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  7. Isolation and Characterization of RNA Aptamers against a Proteasome-Associated Deubiquitylating Enzyme UCH37
    Authors: Jung Hoon Lee
    Chembiochem, 2016;0(0):.
    Applications: Bioassay
  8. Structural and Functional Characterization of Ubiquitin Variant Inhibitors of USP15.
    Authors: Teyra J, Singer A, Schmitges F, Jaynes P, Kit Leng Lui S, Polyak M, Fodil N, Krieger J, Tong J, Schwerdtfeger C, Brasher B, Ceccarelli D, Moffat J, Sicheri F, Moran M, Gros P, Eichhorn P, Lenter M, Boehmelt G, Sidhu S
    Structure, 0;0(0):.
    Species: Human
    Sample Types: Transfected Whole Cells
    Applications: Bioassay


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Recombinant Human Ubiquitin Rhodamine 110 Protein, CF
By Anonymous on 06/01/2019
Application: Enzymatic activity in vitro

Recombinant Human Ubiquitin Rhodamine 110 Protein, CF
By Anonymous on 04/29/2019
Application: Enzymatic activity in vitro