Introduction
Ubiquitin, a highly conserved 76-amino acid protein found in all eukaryotes, exists in various forms: free, monomerically conjugated to proteins, or as ubiquitin chains. While polyubiquitination typically leads to substrate degradation, monoubiquitinated proteins remain stable. Ubiquitination involves a three-step process using a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin protein ligase (E3). The process begins with the transfer of a ubiquitin moiety to the ε-amino group of a lysine residue on the target protein, forming an isopeptide bond. Subsequent ubiquitin moieties are added to Lys48 of the previous ubiquitin, creating a polyubiquitin chain. Importantly, Ubiquitin K48R, with its Lys48 to Arg48 mutation, disrupts polyubiquitin chain formation via Lys48 linkages, limiting conjugation to mono-ubiquitination and preventing substrate degradation.
Description
Recombinant human ubiquitin K48R is designed to limit polyubiquitin chain formation and reduce conjugation rates. By substituting Lys48 with Arg48, this variant alters the ubiquitination process. Produced in E.coli and purified using proprietary chromatographic methods, it offers high purity for research applications.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The protein is supplied in a solution of PBS with 5% glycerol.
Stability
For long-term storage, keep the vial at a temperature between -20°C and -80°C. Under these conditions, the protein remains stable for up to 12 months. Repeated freezing and thawing should be avoided.
Purity
Analysis by SDS-PAGE confirms a purity exceeding 95%.
Synonyms
Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A, Ubiquitin K48R.