U5507
Ubiquitin human
recombinant, expressed in E. coli (N-terminal histidine tagged)
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About This Item
Product Name
Ubiquitin human, recombinant, expressed in E. coli (N-terminal histidine tagged)
biological source
human
recombinant
expressed in E. coli (N-terminal histidine tagged)
assay
≥95% (GE)
form
lyophilized powder
mol wt
10.7 kDa
technique(s)
ligand binding assay: suitable
solubility
Tris-HCl, pH 7.5: 1.0—1.10 mg/mL, clear to slightly hazy, colorless
suitability
suitable for molecular biology
storage temp.
−20°C
Quality Level
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Application
Ubiquitin human can be used as a test compound for studying the isolation and characterization of rice E3-ubiquitin ligase and the role of OsHOS1 gene in the modulation of the cold stress response.
Ubiquitin human has been used:
- as a substrate in in vitro ubiquitination assays
- as substrate in ADP-ribosylation and ubiquitylation assays
- to supplement the 64 ng of endogenous ubiquitin in fresh blood for experiment grouping in order to study its potential clinical impact on cancer prognosis
Biochem/physiol Actions
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.
Ubiquitin plays a key role in normal eukaryotic cell function. It participates in the development and function of the immune system. This immunophilin is also known to participate in immune homeostasis. The ubiquitin peptide fragment (U50-59) is capable of blocking cellular and humoral immunity.
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.
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.
Ubiquitin is a highly conserved protein composed of 76 amino acids, and it is expressed universally in all eukaryotes, ranging from yeast to humans.
Ubiquitin, a globular protein is made of 76 amino acids and has lysine residues on its surface. It has a molecular weight of 8565 Da.N-Terminal histidine-tagged ubiquitin can replace native ubiquitin in the formation of poly-ubiquitin—protein conjugates. The histidine tag enables the separation and enrichment of protein conjugates on a Ni(II) column and the detection of conjugates in western blot by anti-histidine-tag antibodies.
Preparation Note
Ubiquitin human can dissolved in 0.02 M Tris-HCl at a concentration of 1.00 - 1.10 mg/ml to yield a clear to slightly hazy, colorless solution.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Regulation of NF-kappaB by ubiquitination
Chen J and Chen ZJ
Current Opinion in Immunology, 4-12 (2013)
New crystal form of human ubiquitin in the presence of magnesium
Camara-Artigas A, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 72(1), 29-35 (2016)
Tiago Lourenço et al.
Plant molecular biology, 83(4-5), 351-363 (2013-06-20)
Plants can cope with adverse environmental conditions through the activation of stress response signalling pathways, in which the proteasome seems to play an important role. However, the mechanisms underlying the proteasome-mediated stress response in rice are still not fully understood.
Ubiquitin modification by the E3 ligase/ADP-ribosyltransferase Dtx3L/Parp9
Yang CS, et al.
Molecular Cell, 66(4), 503-516 (2017)
Proteomics strategy to identify substrates of LNX, a PDZ domain-containing E3 ubiquitin ligase
Guo Z, et al.
Journal of Proteome Research, 11(10), 4847-4862 (2012)
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