Ubiquitin−Agarose 

Useful tool for the purification of ubiquitin binding proteins. These include, for example, ubiquitin-activating protein E1, ubiquitin carrier proteins E2, ubiquitin-ligases E3, ubiquitin C-terminal hydrolases (isopeptidases), and proteins that bind ubiquitin but do not participate in the proteasome degradation system.
Ubiquitin-agarose affinity resin has been used for isolation and purification of factors of the ubiquitin conjugation system from various eukaryotic organisms such as rabbit, bovine, human, and yeast.

Suspension in 1 M NaCl containing 0.02% thimerosal

saline suspension

7-15 mg per mL

Fast flow highly cross-linked 4% beaded agarose

6 carbon

2-8°C

Ciechanover, A., et al., Covalent affinity purification of ubiquitin-activating enzyme. J. Biol. Chem. 257, 2537-2542, (1982) abstract

Handley, P.M., Molecular cloning sequence and tissue distribution of the human ubiquitin-activating enzyme E1. Proc. Natl. Acad. Sci. USA 88, 258, (1991) abstract

Hershko, A., et al., Components of ubiquitin-protein ligase system. Resolution affinity purification and role in protein breakdown. J. Biol. Chem. 258, 8206, (1983) abstract

Hoefer, M., and Cook, J.C., Purification and partial characterization of ubiquitin-activating enzyme from Saccharomyces cerevisiae. FEBS Lett. 289, 54-59, (1991)

Majetschak, M., et al., The ubiquityl-calmodulin synthetase system from rabbit reticulocytes: isolation of the ubiquitin-binding first component, a ubiquitin-activating enzyme. Eur. J. Biochem. 255, 482-491, (1998) abstract

Wilkinson, K.D., et al., Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T. Biochemistry 34, 14535-14546, (1995) abstract

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