U6253
Ubiquitin from bovine erythrocytes
BioUltra, ≥98% (SDS-PAGE), essentially salt-free, lyophilized powder
Synonym(s):
ATP-dependent proteolytic factor, Ub
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About This Item
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biological source
bovine erythrocytes
product line
BioUltra
Assay
≥98% (SDS-PAGE)
form
essentially salt-free, lyophilized powder
storage condition
(Tightly closed. Dry)
technique(s)
western blot: suitable
impurities
salt, essentially free
solubility
water: 1 mg/mL, clear, colorless
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LOC(101902760)
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General description
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.
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.
Ubiquitin from bovine erythrocytes can be used for in vitro ubiquitinylation assay. The product can also be used as a marker in western blotting.
Biochem/physiol Actions
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.
Preparation Note
Ubiquitin from bovine erythrocytes can dissolved in water at 1 mg/ml to yield a clear, colorless solution.
antibody
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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.
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
Errol W Robinson et al.
Analytical chemistry, 80(19), 7508-7515 (2008-08-30)
Field asymmetric waveform ion mobility spectrometry (FAIMS) has emerged as an analytical tool of broad utility, especially in conjunction with mass spectrometry. Of particular promise is the use of FAIMS and 2-D ion mobility methods that combine FAIMS with conventional
The ubiquitin system for protein degradation.
A Hershko et al.
Annual review of biochemistry, 61, 761-807 (1992-01-01)
Biochemistry, Ubiquitination
Guo HJ, et al.
StatPearls [Internet] (2022)
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