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 (Ub) plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The protein to be degraded is conjugated to Ub and the ubiquinated protein is then selectively degraded by a 26S complex, multicatalytic 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. The recombinant Ubiquitin is expressed from E. coli and purified by proprietary chromatographic techniques.
Source:
Recombinant corresponding to human Ubiquitin expressed in E.coli.
Molecular Weight:
~8kD
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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