Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF
Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF Summary
Product Specifications
Met1 - Gly76
Contains Lys to Arg substitutions at the following positions: 6, 11, 27, 29, 33, 48, 63
Product Datasheets
Carrier Free
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.
UM-NOK
| Formulation | Lyophilized from a solution in deionized water. |
| Reconstitution | Reconstitute at 10 mg/mL in an aqueous solution. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
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 and renders Ubiquitin unable to form isopeptide-linked poly-Ubiquitin chains making it useful as a negative control.
- 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.
Citations for Recombinant Human Ubiquitin Mutant (No Lysine) 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
Filter your results:
Filter by:
-
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, 2022-10-27;13(1):6411.
Species: N/A
Sample Types: Recombinant Protein
Applications: Bioassay -
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, 2021-04-14;592(7856):789-793.
Species: Human
Sample Types: Peptide
Applications: Bioassay -
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, 2017-04-20;169(3):470-482.e13.
Applications: Bioassay -
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, 2017-01-23;0(0):.
Applications: Ubiquitination
FAQs
-
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.
Reviews for Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF
There are currently no reviews for this product. Be the first to review Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF and earn rewards!
Have you used Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image
