The conserved 76 amino acid protein ubiquitin （Ub） regulates a host of intracellular processes through its enzymatic conjugation to other cellular proteins.
Ubiquitination occurs through sequential steps catalyzed by activating （E1）， conjugating （E2）， and ligase （E3） enzymes. The final step results in the formation of an isopeptide bond between Ub’s C-terminal glycine residue （G76） and a lysine residue of the target protein， although N-terminal ubiquitination is also known.
Outcomes of this modification include destabilization of the conjugated protein， altered protein trafficking and functional modulation.
After targeting the protein for specific localizations， ubiquitin is released from the substrate by deubiquitinating enzymes.
A mutant ubiquitin， having a Gly to Ala substitution at the C-terminus （G76A ubiquitin） supported several downstream reactions of the proteolytic pathway but inhibits the deubiquitination process.
As consequence， the Ub derivative becomes irreversibly conjugated to protein， shifting the equilibrium between the bound and unbound form in the direction of conjugation， at the expense of the free form.
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来源宿主
大肠杆菌中重组表达
溶解建议
Sterile Filtered clear solution. Diluted in PBS plus 5% glycerol.
保存建议
Store vial at -20℃ to -80℃. When stored at the recommended temperature， this protein is stable for 12 months.
Please prevent freeze-thaw cycles.
