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Recombinant Human Ubiquitin 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 Protein, CF Summary

Details of Functionality
Recombinant Human Ubiquitin 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). Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human Ubiquitin concentration of 0.01-0.5 mM.
Source
E. coli-derived human Ubiquitin protein
Met1 - Gly76
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
8.6 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
U-100H 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 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).

The Ubiquitin product was processed to eliminate glycine and buffer salts which can interfere with chemical and in vitro reactions.

  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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Publications for Ubiquitin (U-100H)(137)

We have publications tested in 13 confirmed species: Human, Mouse, Bacteria, Bacteria - E. Coli, Bacteria - Escherichia coli, E. coli, N/A, Parasite - Plasmodium falciparum, Plant - Oryza sativa (Rice), Spodoptera frugiperda, Virus - HPV, Xenopus, Yeast - Saccharomyces cerevisiae.

We have publications tested in 7 applications: Binding Assay, Bioassay, ELISA, Enzyme Assay, Ubiquitination, Ubiquitylation, Western Blot.


Filter By Application
Binding Assay
(1)
Bioassay
(113)
ELISA
(1)
Enzyme Assay
(4)
Ubiquitination
(16)
Ubiquitylation
(1)
Western Blot
(1)
All Applications
Filter By Species
Human
(77)
Mouse
(2)
Bacteria
(1)
Bacteria - E. Coli
(2)
Bacteria - Escherichia coli
(1)
E. coli
(2)
N/A
(20)
Parasite - Plasmodium falciparum
(1)
Plant - Oryza sativa (Rice)
(1)
Spodoptera frugiperda
(1)
Virus - HPV
(1)
Xenopus
(1)
Yeast - Saccharomyces cerevisiae
(1)
All Species
Showing Publications 1 - 10 of 137. Show All 137 Publications.
Publications using U-100H Applications Species
Chan, A;Haley, RM;Najar, MA;Gonzalez-Martinez, D;Bugaj, LJ;Burslem, GM;Mitchell, MJ;Tsourkas, A; Lipid-mediated intracellular delivery of recombinant bioPROTACs for the rapid degradation of undruggable proteins Nature communications 2024-07-10 [PMID: 38987546] (Bioassay, Human) Bioassay Human
Wang, S;Li, H;Liu, X;Yin, T;Li, T;Zheng, M;Liu, M;Meng, X;Zhou, J;Wang, Y;Chen, Y; VHL suppresses UBE3B-mediated breast tumor growth and metastasis Cell death & disease 2024-06-24 [PMID: 38914543] (Bioassay, N/A) Bioassay N/A
Kubori, T;Arasaki, K;Oide, H;Kitao, T;Nagai, H; Multi-tiered actions of Legionella effectors to modulate host Rab10 dynamics eLife 2024-05-21 [PMID: 38771316] (Bioassay, N/A) Bioassay N/A
Radko-Juettner, S;Yue, H;Myers, JA;Carter, RD;Robertson, AN;Mittal, P;Zhu, Z;Hansen, BS;Donovan, KA;Hunkeler, M;Rosikiewicz, W;Wu, Z;McReynolds, MG;Roy Burman, SS;Schmoker, AM;Mageed, N;Brown, SA;Mobley, RJ;Partridge, JF;Stewart, EA;Pruett-Miller, SM;Nabet, B;Peng, J;Gray, NS;Fischer, ES;Roberts, CWM; Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing SWI/SNF Nature 2024-03-27 [PMID: 38538798] (Bioassay, N/A) Bioassay N/A
Wang, JCK;Baddock, HT;Mafi, A;Foe, IT;Bratkowski, M;Lin, TY;Jensvold, ZD;Preciado López, M;Stokoe, D;Eaton, D;Hao, Q;Nile, AH; Structure of the p53 degradation complex from HPV16 Nature communications 2024-02-28 [PMID: 38418456] (Bioassay, Bacteria - Escherichia coli) Bioassay Bacteria - Escherichia coli
Wu, K;DeVita, RJ;Pan, ZQ; Mono-ubiquitination empowers ubiquitin chain elongation The Journal of biological chemistry 2024-02-12 [PMID: 38354782] (Bioassay, Human) Bioassay Human
Zhu, K;Suskiewicz, MJ;Chatrin, C;Strømland, Ø;Dorsey, BW;Aucagne, V;Ahel, D;Ahel, I; DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids Nucleic acids research 2023-11-24 [PMID: 38000390] (Bioassay, N/A) Bioassay N/A
Tian, T;Xie, X;Yi, W;Zhou, Y;Xu, Y;Wang, Z;Zhang, J;Lin, M;Zhang, R;Lv, Z;Li, X;Lv, L;Xu, Y; FBXO38 mediates FGL1 ubiquitination and degradation to enhance cancer immunity and suppress inflammation Cell reports 2023-11-28 [PMID: 37938970] (Bioassay, N/A) Bioassay N/A
Li, P;Zhen, Y;Kim, C;Liu, Z;Hao, J;Deng, H;Deng, H;Zhou, M;Wang, XD;Qin, T;Yu, Y; Nimbolide targets RNF114 to induce the trapping of PARP1 and synthetic lethality in BRCA-mutated cancer Science advances 2023-10-27 [PMID: 37878693] (Bioassay, Human) Bioassay Human
VanDyke, D;Xu, L;Sargunas, PR;Gilbreth, RN;Baca, M;Gao, C;Hunt, J;Spangler, JB; Redirecting the specificity of tripartite motif containing-21 scaffolds using a novel discovery and design approach The Journal of biological chemistry 2023-10-20 [PMID: 37866632] (Bioassay, N/A) Bioassay N/A
Show All 137 Publications.

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Ubiquitin-Mediated Degradation of Cellular Proteins: The Kiss of Death
Ubiquitin is an abundant and essential cellular 9-kd protein that is conserved across evolution from yeast to humans. Ubiquitin is used by cells as a covalent modifier of other proteins both to activate their function and to target them for degradatio...  Read full blog post.

Using Ubiquitin Antibodies in Various Disease Research
Ubiquitin is a small, highly conserved protein which plays an important role in protein breakdown, covalently bonding to proteins to mark them for proteolytic degradation in a process called ubiquitination. Ubiquitin also binds to inclusion bodies (ac...  Read full blog post.

The Heat is On: Heat Shock Proteins and the Link to Cancer
Novus Biologicals offers an extensive antibody catalog targeting heat shock proteins (HSPs). A large protein group covering a number of families, the HSPs are functionally related by their dramatic upregulation in response to stress. Stress triggers m...  Read full blog post.

The Latest Research on IBR-type E3 Ubiquitin Ligases
E3 ubiquitin ligases are standards in most antibody catalogs. These proteins are essential to the process of ubiquitination, which is expressed in protein pathways throughout the body and is often linked to disease states. It is widely used as a bioma...  Read full blog post.

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Bioinformatics

Gene Symbol UBB
Uniprot