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UBB; Ubiquitin B

Protein

E. coli

Human ubiquitin K48R mutant (Accession Nr. P0CG47) fused to a N-terminal His-tag.

Human

~9.3kDa

≥95% (SDS-PAGE)

Soluble and stable aqueous buffers up to 10mg/ml.

Lyophilized.

Use: Mutation of lysine 48 to arginine renders ubiquitin unable to form poly-ubiquitin chains via lysine 48 linkages with other ubiquitin molecules. Can form a ubiquitin-activating (E1) enzyme-catalyzed active thioester at the C-terminus allowing the molecule to be transferred to the lysines of substrate proteins (mono-ubiquitination). Ideal for investigating biological processes involving a particular ubiquitin chain linkage. This mutant K48R prevents the formation of K48-linked ubiquitin chains. Ideal for the reduction in poly-ubiquitin chain length/conjugation rates and for the determination of poly-ubiquitin chains specificity. Reaction conditions will need to be optimized for each specific application. Typical concentrations for non rate-limiting support of in vitro conjugation reactions range from 0.2-1mM depending on experimental conditions.

Manufactured by Boston Biochem

BLUE ICE

+4°C

-20°C

Aliquot to avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -20°C.

No

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Ubiquitin is a 76 amino acid (aa) protein that is ubiquitously expressed in all eukaryotic organisms. ubiquitin is highly conserved with 96% aa sequence identity shared between human and yeast ubiquitin, and 100% aa sequence identity shared between human and mouse ubiquitin. In mammals, four ubiquitin genes encode for two ubiquitin-ribosomal fusion proteins and two poly-ubiquitin proteins. Cleavage of the ubiquitin precursors by deubiquitinating enzymes gives rise to identical ubiquitin monomers each with a predicted molecular weight of 8.6 kDa. Conjugation of ubiquitin to target proteins involves the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and a lysine residue in the target protein. This process of conjugation, referred to as ubiquitination or ubiquitylation, is a multi-step process that requires three enzymes: a ubiquitin-activating (E1) enzyme, a ubiquitin-conjugating (E2) enzyme, and a ubiquitin ligase (E3). ubiquitination is classically recognized as a mechanism to target proteins for degradation and as a result, ubiquitin was originally named ATP-dependent Proteolysis Factor 1 (APF-1). In addition to protein degradation, ubiquitination has been shown to mediate a variety of biological processes such as signal transduction, endocytosis, and post-endocytic sorting.

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