U5382
Ubiquitin human
≥95% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal FLAG® tagged), lyophilized powder
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biological source
human
Quality Level
recombinant
expressed in E. coli (N-terminal FLAG® tagged)
assay
≥95% (SDS-PAGE)
form
lyophilized powder
mol wt
10 kDa
technique(s)
mass spectrometry (MS): suitable
solubility
0.05 M Tris pH 7.5: ≥10 mg/mL
storage temp.
−20°C
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General description
Ubiquitin is a highly conserved globular protein and has lysine in the surface. The C-terminal end comprises the Leu-Arg-Gly-Gly structural motif.
Application
Ubiquitin human can be used as a standard for mass spectrometry.
Ubiquitin human has been used in mono-ubiquitination of yeast proliferating cell nuclear antigen (PCNA) and in in vitro ubiquitination assay of defective in mitotic arrest 1 (Dma1)
Ubiquitin, N-terminal FLAG-tagged can replace the ubiquitin in formation of poly-ubiquitin—protein conjugates. The FLAG tag enables separation and enrichment of the protein conjugates on anti-FLAG affinity columns and detection of conjugates in western blot by anti-FLAG antibodies.
Biochem/physiol Actions
Ubiquitin interacts with the lysine residue of proteins through its ε-amino group of the C-terminal glycine residue. Proteins interacting with ubiquitin either undergo mono-ubiquitination or multi-mono-ubiquitination via a three-step process. Ubiquitination regulates intracellular trafficking and protein degradation and an imbalance in the pathway is implicated in disorders.
Ubiquitin is a small regulatory protein present in eukaryote tissues. Exogenous ubiquitin can stimulate apoptosis in numerous cell lines. E7 protein of human papilloma virus-16 stimulates Retinoblastoma Protein degradation via Ubiquitin-Proteasome Pathway.
Packaging
Package size based on protein content
Preparation Note
Ubiquitin human can be dissolved in 0.05 M Tris-HCl at a concentration of 10.00 - 11.00 mg/ml to yield a clear to slightly hazy, colorless solution.
Legal Information
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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Acta crystallographica. Section F, Structural biology communications, 72(Pt 1), 29-35 (2016-01-12)
Ubiquitin is a small globular protein that has a considerable number of lysine residues on its surface. This results in a high surface entropy that precludes the formation of crystal-packing interactions. To date, only a few structures of the native
Biochemical Society transactions, 37(Pt 5), 937-953 (2009-09-17)
Protein ubiquitination and protein phosphorylation are two fundamental regulatory post-translational modifications controlling intracellular signalling events. However, the ubiquitin system is vastly more complex compared with phosphorylation. This is due to the ability of ubiquitin to form polymers, i.e. ubiquitin chains
Molecular & cellular proteomics : MCP, 5(5), 949-958 (2006-02-16)
Top-down proteomics, the analysis of intact proteins (instead of first digesting them to peptides), has the potential to become a powerful tool for mass spectrometric protein characterization. Requirements for extremely high mass resolution, accuracy, and ability to efficiently fragment large
The Journal of biological chemistry, 288(7), 4704-4714 (2012-12-25)
Progression through the G(1) phase of the cell cycle is controlled by diverse cyclin-dependent kinases (CDKs) that might be associated to numerous cyclin isoforms. Given such complexity, regulation of cyclin degradation should be crucial for coordinating progression through the cell
Cancer research, 56(20), 4620-4624 (1996-10-15)
Rb protein is a critical regulator of entry into the cell cycle, and loss of Rb function by deletions, mutations, or interaction with DNA viral oncoproteins leads to oncogenic transformation. We have shown that the human papilloma virus (HPV)-16 E7
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