Recombinant Human Ubiquitin Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Enzyme Activity

Order Details

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.
E. coli-derived human Ubiquitin protein
Accession #
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.


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.
Read Publications using
U-100H in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a solution in deionized water.
>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.


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


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).

Highly purified Ubiquitin processed for the quantitative removal of 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)(57)

We have publications tested in 4 confirmed species: Human, Bacteria - E. Coli, N/A, Saccharomyces cerevisiae.

We have publications tested in 8 applications: Binding Assay, Bioassay, ELISA, EnzAct, Enzyme Assay, Ubiquitination, enzymatic assay, in vitro ubiquitination.

Filter By Application
Binding Assay
Enzyme Assay
enzymatic assay
in vitro ubiquitination
All Applications
Filter By Species
Bacteria - E. Coli
Saccharomyces cerevisiae
All Species
Showing Publications 1 - 10 of 57. Show All 57 Publications.
Publications using U-100H Applications Species
X Huang, XN Wang, XD Yuan, WY Wu, PE Lobie, Z Wu XIAP facilitates breast and colon carcinoma growth via promotion of p62 depletion through ubiquitination-dependent proteasomal degradation Oncogene, 2018;0(0):. 2018 [PMID: 30275562] (Bioassay, Human) Bioassay Human
KA Donovan, J An, RP Nowak, JC Yuan, EC Fink, BC Berry, BL Ebert, ES Fischer Thalidomide promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray syndrome Elife, 2018;7(0):. 2018 [PMID: 30067223] (Ubiquitination, Human) Ubiquitination Human
X Hou, FC Fiesel, D Truban, M Castanedes, WL Lin, AI Soto, P Tacik, LG Rousseau, NN Diehl, MG Heckman, O Lorenzo-Be, I Ferrer, JM Arbelo, JC Steele, MJ Farrer, M Cornejo-Ol, L Torres, IF Mata, NR Graff-Radf, ZK Wszolek, OA Ross, ME Murray, DW Dickson, W Springer Age- and disease-dependent increase of the mitophagy marker phospho-ubiquitin in normal aging and Lewy body disease Autophagy, 2018;14(8):1404-1418. 2018 [PMID: 29947276] (Bioassay) Bioassay
S Ito, A Ueno, T Ueda, H Nakagawa, H Taniguchi, N Kayukawa, A Fujihara-I, F Hongo, K Okihara, O Ukimura CNPY2 inhibits MYLIP-mediated AR protein degradation in prostate cancer cells Oncotarget, 2018;9(25):17645-17655. 2018 [PMID: 29707137] (Bioassay) Bioassay
D Valleau, AT Quaile, H Cui, X Xu, E Evdokimova, C Chang, ME Cuff, ML Urbanus, S Houliston, CH Arrowsmith, AW Ensminger, A Savchenko Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophila Cell Rep, 2018;23(2):568-583. 2018 [PMID: 29642013] (Bioassay) Bioassay
LJ Albee, HM LaPorte, X Gao, JM Eby, YH Cheng, AM Nevins, BF Volkman, V Gaponenko, M Majetschak Identification and functional characterization of arginine vasopressin receptor 1A : atypical chemokine receptor 3 heteromers in vascular smooth muscle Open Biol, 2018;8(1):. 2018 [PMID: 29386406] (Bioassay, Human) Bioassay Human
SY Kim, HJ Kim, HJ Kim, DH Kim, CH Kim, JH Han, HK Byeon, K Lee HSPA5 negatively regulates lysosomal activity through ubiquitination of MUL1 in head and neck cancer Autophagy, 2017;0(0):1-89. 2017 [PMID: 29260979] (Bioassay, Human) Bioassay Human
C Yang, W Zang, Z Tang, Y Ji, R Xu, Y Yang, A Luo, B Hu, Z Zhang, Z Liu, X Zheng A20 regulates the DNA damage response and mediates tumor cell resistance to DNA damaging therapy Cancer Res., 2017;0(0):. 2017 [PMID: 29233925] (Bioassay, Human) Bioassay Human
JB Hein, EPT Hertz, DH Garvanska, T Kruse, J Nilsson Distinct kinetics of serine and threonine dephosphorylation are essential for mitosis Nat. Cell Biol., 2017;19(12):1433-1440. 2017 [PMID: 29084198] (Bioassay, Human) Bioassay Human
M Boselli, BH Lee, J Robert, MA Prado, SW Min, C Cheng, MC Silva, C Seong, S Elsasser, KM Hatle, TC Gahman, SP Gygi, SJ Haggarty, L Gan, RW King, D Finley An inhibitor of the proteasomal deubiquitinating enzyme USP14 induces tau elimination in cultured neurons J. Biol. Chem., 2017;0(0):. 2017 [PMID: 28972160] (EnzAct, Human) EnzAct Human
Show All 57 Publications.

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Blogs on Ubiquitin.

There's an autophagy for that!
By Christina Towers, PhDA critical mechanism that cells use to generate nutrients and fuel metabolism is through a process called autophagy.  This process is complex and involves over 20 different proteins, most of which are highly conserved acro...  Read full blog post.

Article Review: Glucose-induced transcriptional regulation in cancer
Epigenetic mechanisms have been implicated in many physiological and pathophysiological processes. Among these, histone modifications including methylation, phosphorylation, acetylation and ubiquitination, significantly modify gene expression. In c...  Read full blog post.

PINK1: All work and no fun
The protein PINK1 is a mitochondrial-located serine/threonine kinase (PTK) that maintains organelle function and integrity. It not only protects organelles from cellular stress, but it also uses the selective auto-phagocytosis process for cleaning and...  Read full blog post.

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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Gene Symbol UBB