Recombinant Human His6-Ubiquitin Mutant K11R Protein, CF

Recombinant Human His6-Ubiquitin Mutant K11R Protein, 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).

Mutation of lysine 11 to arginine renders Ubiquitin unable to form poly-Ubiquitin chains via lysine11 linkages with other Ubiquitin molecules. Ubiquitin K11R 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. Ideal for the reduction in poly-Ubiquitin chain length/conjugation rates and determining if poly-Ubiquitin chains are K11 linked.

Related Research Areas

• Cell Structure and Signaling Molecules
• Cell to Cell Adhesion Disassembly During EMT
• HIF Transcription Factors
• Negative Regulators of the Jak/STAT Pathway
• Neurofibrillary Tangle Formation
• NFkB Pathway
• Notch Pathway
• Parkinson's Disease Related Molecules
• Ubiquitin
• Ubiquitin-related Molecules in the Akt Pathway
• Wnt Intracellular Signaling