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U6253

Sigma-Aldrich

Ubiquitin from bovine erythrocytes

BioUltra, ≥98% (SDS-PAGE), essentially salt-free, lyophilized powder

Synonyme(s) :

ATP-dependent proteolytic factor, Ub

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About This Item

Numéro CAS:
79586-22-4
Numéro MDL:
MFCD00082121
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

bovine erythrocytes

Gamme de produits

BioUltra

Pureté

≥98% (SDS-PAGE)

Forme

essentially salt-free, lyophilized powder

Conditions de stockage

(Tightly closed. Dry)

Technique(s)

western blot: suitable

Impuretés

salt, essentially free

Solubilité

water: 1 mg/mL, clear, colorless

Numéro d'accès UniProt

P0CG48

Température de stockage

2-8°C

Informations sur le gène

bovine ... LOC(101902760)

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Catégories apparentées

Description générale

Research area: Cancer

Ubiquitin is a highly conserved regulatory protein. It is found in all eukaryotic cells and is virtually identical across all forms of life including yeast, humans, and plants. ubiquitin structure contains seven Lys residues and an N-terminus, all of which are target sites for ubiquitination.

Application

Ubiquitin from bovine erythrocytes has been used to study the role of exogenous ubiquitin in chronic β-adrenergic receptor (β-AR)-stimulated myocardial remodeling. It has also been used to test the inhibitor of nuclear factor kappa-B kinase subunit beta (IKKβ) ubiquitylation.

Ubiquitin from bovine erythrocytes can be used for in vitro ubiquitinylation assay. The product can also be used as a marker in western blotting.

Actions biochimiques/physiologiques

Ubiquitination is a post-translational modification process where ubiquitin-protein is attached to a substrate protein. Ubiquitination plays a vital role in the regulation of cellular signaling in various biological processes such as apoptosis, protein processing, immune response, and DNA repair. Ubiquitination mediates protein degradation via the ubiquitin-proteasome pathway. Ubiquitination is implicated in various cellular signaling pathways. Polyubiquitination modulates the signal activation of NF-κ-B inhibitor alpha (IkB-α) in the inflammatory signaling pathway. Elevated levels of ubiquitin have been observed in various diseases such as parasitic and allergic diseases, alcoholic liver disease, type 2 diabetes, β2-microglobulin amyloidosis, and chronic hemodialysis.

Notes préparatoires

Ubiquitin from bovine erythrocytes can dissolved in water at 1 mg/ml to yield a clear, 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)

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Guo HJ, et al.
StatPearls [Internet] (2022)
Christopher R Daniels et al.
American journal of physiology. Heart and circulatory physiology, 303(12), H1459-H1468 (2012-10-09)
β-Adrenergic receptor (β-AR) stimulation increases extracellular ubiquitin (UB) levels, and extracellular UB inhibits β-AR-stimulated apoptosis in adult cardiac myocytes. This study investigates the role of exogenous UB in chronic β-AR-stimulated myocardial remodeling. l-Isoproterenol (ISO; 400 μg·kg(-1)·h(-1)) was infused in mice
A L Schwartz et al.
Annual review of medicine, 50, 57-74 (1999-03-12)
The ubiquitin-proteasome pathway plays a pivotal role in the degradation of short-lived and regulatory proteins important in a variety of basic cellular processes, including regulation of the cell cycle, modulation of cell surface receptors and ion channels, and antigen presentation.
The ubiquitin system for protein degradation.
A Hershko et al.
Annual review of biochemistry, 61, 761-807 (1992-01-01)
Takeshi Miura et al.
FEMS microbiology letters, 239(1), 171-179 (2004-09-29)
When Saccharomyces cerevisiae cells are exposed to high hydrostatic pressure, tryptophan permease Tat2 is degraded in a manner dependent on Rsp5 ubiquitin ligase. Consequently, cell growth is arrested in tryptophan auxotrophic strains. Here we show that of 17 ubiquitin-specific protease
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