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Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF Summary

Additional Information
Soon to be discontinued.
Details of Functionality
Recombinant Human Ubiquitin Mutant (No Lysine) 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 Lysine) 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 Lysine) concentration of 0.2-1 mM.
Source
E. coli-derived human Ubiquitin protein
Met1 - Gly76
Contains Lys to Arg substitutions at the following positions: 6, 11, 27, 29, 33, 48, 63
Accession #
Protein/Peptide Type
Recombinant Proteins
Gene
UBB
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
8.8 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
UM-NOK in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a solution in deionized water.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Reconstitution Instructions
Reconstitute at 10 mg/mL in an aqueous solution.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Ubiquitin Mutant (No Lysine) Protein, CF

  • RPS27A
  • UBA52
  • UBB ubiquitin B
  • UBB
  • UBC
  • Ubiquitin

Background

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.

  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.

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UM-NOK
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Publications for Ubiquitin (UM-NOK)(4)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 2 applications: Bioassay, Ubiquitination.


Filter By Application
Bioassay
(3)
Ubiquitination
(1)
All Applications
Filter By Species
Human
(1)
N/A
(1)
All Species

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Bioinformatics

Gene Symbol UBB
Uniprot