U5507
Ubiquitin human
recombinant, expressed in E. coli (N-terminal histidine tagged)
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About This Item
Polecane produkty
pochodzenie biologiczne
human
Poziom jakości
rekombinowane
expressed in E. coli (N-terminal histidine tagged)
Próba
≥95% (GE)
Postać
lyophilized powder
masa cząsteczkowa
10.7 kDa
metody
ligand binding assay: suitable
rozpuszczalność
Tris-HCl, pH 7.5: 1.0—1.10 mg/mL, clear to slightly hazy, colorless
przydatność
suitable for molecular biology
temp. przechowywania
−20°C
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Opis ogólny
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.
Zastosowanie
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
Działania biochem./fizjol.
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.
Uwaga dotycząca przygotowania
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.
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Kod klasy składowania
11 - Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Gloves, type N95 (US)
Certyfikaty analizy (CoA)
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Klienci oglądali również te produkty
Regulation of NF-kappaB by ubiquitination
Chen J and Chen ZJ
Current Opinion in Immunology, 4-12 (2013)
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.
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)
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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