Recombinant Human Ubiquitin w/K48 only N-Term Biotin, CF

Recombinant Human Ubiquitin w/K48 only N-Term Biotin, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Ubiquitin

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 (1). 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) (2,3). 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 (4-7).

Produced via a proprietary process resulting in a single Biotin modification exclusively on the N-terminus of Ubiquitin. This site-specific modification results in a Ubiquitin that is fully functional at the C-terminus, and with the full compliment of reactive lysines to allow for poly-Ubiquitin chain incorporation. Detection with Avidin-linked reagents allows for a higher efficiency and detection sensitivity than with Anti-Ubiquitin antibodies. Ideal as an alternative Toradio-labeled 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.

Related Research Areas

• Cell Structure and Signaling Molecules
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• Parkinson's Disease Related Molecules
• Ubiquitin
• Ubiquitin-related Molecules in the Akt Pathway
• Wnt Intracellular Signaling