UBE2I Human His

Ubiquitin-Conjugating Enzyme E2I, also known as UBC9, is a crucial enzyme in the ubiquitin-proteasome system, which is responsible for protein degradation and regulation within cells. The human recombinant version of this enzyme, tagged with a His (histidine) tag, is widely used in research to study its function and interactions.

The UBE2I gene encodes the UBC9 protein, which belongs to the ubiquitin-conjugating enzyme family. The human recombinant UBC9 is produced in E. coli and typically includes a His tag for purification purposes. This recombinant protein has a molecular weight of approximately 19.5 kDa and consists of 171 amino acids .

UBC9 plays a pivotal role in the second step of the ubiquitination process. In this process, ubiquitin, a small regulatory protein, is first activated by an E1 enzyme. The activated ubiquitin is then transferred to the active site cysteine residue of the E2 enzyme, UBC9. UBC9 subsequently interacts with an E3 ligase, which facilitates the transfer of ubiquitin to target proteins .

Apart from its role in ubiquitination, UBC9 is also involved in SUMOylation, a process similar to ubiquitination but involving Small Ubiquitin-like Modifier (SUMO) proteins. UBC9 accepts SUMO proteins from the E1 complex and catalyzes their attachment to target proteins. This modification can alter the function, localization, or stability of the target proteins .

The human recombinant UBC9 with a His tag is extensively used in biochemical and structural studies. The His tag allows for easy purification of the protein using affinity chromatography. Researchers use this recombinant protein to investigate the mechanisms of ubiquitination and SUMOylation, as well as to identify potential therapeutic targets for diseases related to protein misregulation .