A protein marked for degradation is covalently attached to multiple molecules of ubiquitin, a highly conserved 76 aa (8.6 kda) protein, which escorts it for rapid hydrolysis to the 26S proteasome.
The ubiquitin-proteasome pathway has been implicated in several forms of malignancy, in the pathogenesis of several genetic diseases, and in the pathology of muscle wasting. It is also involved in the destruction of proteins that participate in cell cycle progression, transcription control, signal transduction, proliferation, apoptosis and metabolic regulation.
Millipore’s tools for studying ubiquitin signaling have helped immensely in understanding the biological role and importance of the ubiquitin-proteasome pathway. Millipore is also the first provider of lead discovery services to target the ubiquitination pathway: visit www.millipore.com/ubiquitinprofiler.
 Ubiquitin is a polypeptide of 76 amino acid residues, being a very highly conserved and widely distributed protein in all eukaryotic cells. In these processes, ubiquitin functions as both a signal for protein degradation and as a chaperone promoting the formation of organelles. Recognizes mono- and poly ubiquitinylated proteins, but not free ubiquitin. |  Ubiquitin is a polypeptide of 76 amino acid residues, being a very highly conserved and widely distributed protein in all eukaryotic cells. In these processes, ubiquitin functions as both a signal for protein degradation and as a chaperone promoting the formation of organelles. Recognizes only poly-ubiquitinylated proteins and not mono-ubiquitinylated proteins or free ubiquitin. |
