Recombinant Human Ubiquitin Rhodamine 110 Protein, CF
Recombinant Human Ubiquitin Rhodamine 110 Protein, CF Summary
Contains a C-terminal Rhodamine 110 (R110)
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.
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.
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.
- Sharp, P.M. & W.-H. Li. (1987) Trends Ecol. Evol. 2:328.
- Ciechanover, A. et al. (1980 ) Proc. Natl. Acad. Sci. USA 77:1365.
- Hershko, A. et al. (1980) Proc. Natl. Acad. Sci. USA 77:1783.
- Greene, W. et al. (2012) PLoS Pathog. 8:e1002703.
- Tong, X. et al. (2012) J. Biol. Chem. 287:25280.
- Wei, W. et al. (2004) Nature 428:194.
- Wertz, I.E. et al. (2004) Nature 430:694.
- Hassiepen, U. et al. (2007) Anal. Biochem. 371: 201.
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.
Citations: Showing 1 - 8
Filter your results:
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.
Sample Types: Whole Cells
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.
Sample Types: Cell Lysates
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.
Sample Types: Protein
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):.
Sample Types: Cell Lysates
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):.
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
Sample Types: Recombinant Protein
Isolation and Characterization of RNA Aptamers against a Proteasome-Associated Deubiquitylating Enzyme UCH37
Authors: Jung Hoon Lee
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
Sample Types: Transfected Whole Cells
No product specific FAQs exist for this product, however you mayView all Proteins and Enzyme FAQs
Reviews for Recombinant Human Ubiquitin Rhodamine 110 Protein, CF
Average Rating: 4.5 (Based on 2 Reviews)
Have you used Recombinant Human Ubiquitin Rhodamine 110 Protein, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥1250 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image