U5507
Ubiquitin human
recombinant, expressed in E. coli (N-terminal histidine tagged)
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About This Item
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in E. coli (N-terminal histidine tagged)
Pureté
≥95% (GE)
Forme
lyophilized powder
Poids mol.
10.7 kDa
Technique(s)
ligand binding assay: suitable
Solubilité
Tris-HCl, pH 7.5: 1.0—1.10 mg/mL, clear to slightly hazy, colorless
Adéquation
suitable for molecular biology
Température de stockage
−20°C
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Description générale
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.
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
Actions biochimiques/physiologiques
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.
Notes préparatoires
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.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
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.
Regulation of NF-kappaB by ubiquitination
Chen J and Chen ZJ
Current Opinion in Immunology, 4-12 (2013)
Extracellular Ubiquitin is the Causal Link between Stored Blood Transfusion Therapy and Tumor Progression in a Melanoma Mouse Model
Zhang J, et al.
Journal of Cancer, 10(12), 2822-2835 (2019)
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)
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