U5632
Ubiquitin−Agarose
saline suspension
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About This Item
Produits recommandés
Forme
saline suspension
Niveau de qualité
Ampleur du marquage
7-15 mg per mL
Technique(s)
affinity chromatography: suitable
Matrice
Fast flow highly cross-linked 4% beaded agarose
Espaceur de matrice
6 carbon
Température de stockage
2-8°C
Application
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.
Forme physique
Suspension in 1 M NaCl containing 15 Mm Sodium azide.
Code de la classe de stockage
10 - Combustible liquids
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
Certificats d'analyse (COA)
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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
Hyoung Tae Kim et al.
Methods in molecular biology (Clifton, N.J.), 832, 639-652 (2012-02-22)
The biological role and fates of ubiquitin (Ub) conjugates are determined by the nature of the ubiquitin chain formed on the protein. Recently, we reported that Ring-finger and U-box ubiquitin ligases (E3s), when functioning with different E2s, synthesize different types
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
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
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