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UBB; Ubiquitin B

Protein

E. coli

Human ubiquitin w/K48 (Accession Nr. P0CG47) fused to a His-tag and conjugated to a N-terminal biotin (single modification). Contains only a single lysine (K48) with all other lysines mutated to arginine.

Human

Biotin

Lyophilized from a solution in deionized water.

Use: Allows for poly-ubiquitin chain incorporation of Biotin-N-terminal ubiquitin with higher efficiency and detection sensitivity than traditionally modified Biotin-ubiquitin. Produced via a proprietary process resulting in a single biotin modification exclusively on the N-terminus of ubiquitin. This ubiquitin mutant contains only a single lysine (K48) with all other lysines mutated to arginine, and is able to form poly-ubiquitin chains with other ubiquitin molecules via the K48 lysine only. Ideal as an alternative to radio-labeled ubiquitin, poly-ubiquitin chain visualization/quantitation can be performed via avidin-linked detection. Depending on desired signal strength and assay conditions, Biotin-N-term-ubiquitin should be used in conjunction with native ubiquitin at combined concentration range of 10-50μM with a 1:2 to 1:20 ratio of Biotin-N-term-ubiquitin: native ubiquitin, respectively. Typical amounts for a 20μl reaction: 250ng to 2µg Biotin-N-term-ubiquitin, 5µg native ubiquitin.

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.