Ubiquitin is a small, evolutionarily conserved eukaryotic protein that can be attached to a wide variety of intracellular proteins including itself. Covalent attachment of ubiquitin to other proteins serves various functions, but its major role is to target cellular proteins for destruction. Cellular components that activate, transfer, remove, or simply recognize ubiquitin number in the hundreds, perhaps even in the thousands. In light of this complexity the ubiquitin pathway is ideal for a systems biology approach. Ubiquitin plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The protein to be degraded is conjugated to ubiquitin and the ubiquinated protein is then selectively degraded by a 26S complex, multi-catalytic cytosolic and nuclear protease termed proteasome. The Ub-proteasome proteolytic pathway, which is a complex process, is implicated to be of great importance for regulating numerous cellular processes.||Source:|Recombinant protein corresponding to human Ubiquitin, expressed in E. coli. ||Molecular Weight: |~8.56kD||Storage and Stability:|Aliquot to avoid repeated freezing and thawing and store at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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