U5382
Ubiquitin human
Ubiquitin human
≥95% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal FLAG® tagged), lyophilized powder
Sign Into View Organizational & Contract Pricing
All Photos(1)
Select a Size
Change View
1 MG
$397.00
About This Item
Recommended Products
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, clear to slightly hazy, colorless
0.05 M Tris pH 7.5: ≥10 mg/mL
storage temp.
−20°C
Looking for similar products? Visit Product Comparison Guide
General description
Research Area: CANCER
Ubiquitin is a highly conserved protein composed of 76 amino acids, and it is expressed universally in all eukaryotes, ranging from yeast to humans.[1]
Ubiquitin is a highly conserved protein composed of 76 amino acids, and it is expressed universally in all eukaryotes, ranging from yeast to humans.[1]
Application
Ubiquitin human can be used as a standard for mass spectrometry.[4]
Ubiquitin human has been used in mono-ubiquitination of yeast proliferating cell nuclear antigen (PCNA)[5] and in in vitro ubiquitination assay of defective in mitotic arrest 1 (Dma1)[6]
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.[7]
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.[3] Ubiquitination regulates intracellular trafficking and protein degradation and an imbalance in the pathway is implicated in disorders.[2]
Ubiquitin is a small regulatory protein present in eukaryote tissues. Exogenous ubiquitin can stimulate apoptosis in numerous cell lines.[8] E7 protein of human papilloma virus-16 stimulates Retinoblastoma Protein degradation via Ubiquitin-Proteasome Pathway.[9]
Ubiquitin-mediated proteolysis plays an important role in several basic cellular processes including regulation of cell cycle and division, differentiation and development, modulation of cell-surface receptors, the secretory pathway (protein transport), morphogenesis of neuronal networks, transcriptional regulation and signal transduction, transcriptional silencing, DNA repair, long-term memory, and circadian rhythms.[10]
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
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Certificates of Analysis (COA)
Lot/Batch Number
Don't see the Right Version?
If you require a particular version, you can look up a specific certificate by the Lot or Batch number.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability
Strous, Ger J and van Kerkhof, Peter
Molecular and cellular endocrinology, 143-151 (2002)
The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability
Strous, Ger J and van Kerkhof, Peter
Molecular and Cellular Endocrinology, 143-151 (2002)
Ana Camara-Artigas et al.
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
David Komander
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
Regulation of NF-kappaB by ubiquitination
Chen J and Chen ZJ
Current Opinion in Immunology, 4-12 (2013)
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service
