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U5632
Ubiquitin−Agarose
saline suspension
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1 ML
342,00 €
342,00 €
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1 ML
342,00 €
About This Item
342,00 €
Check Cart for Availability
Empfohlene Produkte
Form
saline suspension
Qualitätsniveau
Kennzeichnungsgrad
7-15 mg per mL
Methode(n)
affinity chromatography: suitable
Matrix
Fast flow highly cross-linked 4% beaded agarose
Matrix-Spacer
6 carbon
Lagertemp.
2-8°C
Anwendung
Ubiquitin-agarose is used in affinity chromatography, protein chromatography, intracellular protein degradation, calpain and lysosomal proteases, proteomics, specialty resins and ubiquitination analysis. Ubiquitin-agarose has been used in a study to produce evidence for a particulate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in the rabbit brain. Ubiquitin-agarose has also been used to study fertilization of the ascidian, Halocynthia roretzi.
Physikalische Form
Suspension in 1 M NaCl, enthält 0.02% Thiomersal
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves
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Shin-Chung Kang et al.
The Journal of pathology, 203(1), 603-608 (2004-04-20)
Although the key event in the pathology of prion diseases is thought to be the conversion of cellular prion protein (PrP(C)) to the protease-resistant scrapie species termed PrP(Sc), the factors that contribute to neurodegeneration in scrapie-infected animals are poorly understood.
Anjali Joshi et al.
Traffic (Copenhagen, Denmark), 9(11), 1972-1983 (2008-09-27)
Retroviral Gag polyprotein precursors are both necessary and sufficient for the assembly and release of virus-like particles (VLPs) from infected cells. It is well established that small Gag-encoded motifs, known as late domains, promote particle release by interacting with components
M Majetschak et al.
European journal of biochemistry, 255(2), 482-491 (1998-08-26)
Ubiquitin is often implicated as a specific tag for protein degradation via the ubiquitin system although only a limited number of physiological proteins have been shown to be degraded in their native tissues via this pathway in vivo. Ubiquitin may
M Hoefer et al.
FEBS letters, 289(1), 54-58 (1991-09-02)
Ubiquitin-activating enzyme was purified from the yeast Saccharomyces cerevisiae by covalent affinity chromatography on ubiquitin-Sepharose followed by HPLC anion-exchange chromatography. Enzyme activity was monitored by the ubiquitin-dependent ATP: 32PPi exchange assay. The purified enzyme has a specific activity of 1.5
A Ciechanover et al.
The Journal of biological chemistry, 257(5), 2537-2542 (1982-03-10)
We have previously described an enzyme that activates ubiquitin, the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes (Ciechanover, A., Heller, H., Katz-Etzion, R., and Hershko, A. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 761-765). It carries
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