UBE1 Protein, active, 10 µg

Ubiquitination Cascade Comoponent: E1

UBE1 has a crucial function in initiating the ubiquitin-proteasome pathway by activating ubiquitin. Research has shown that purified UBE1 can activate and link UB to ubiquitin-conjugating enzyme E2s. The substantial quantity of purified UBE1 is valuable for in vitro research on the ubiquitin pathway and its structural studies.

Ubiquitin activating enzyme E1 (UBE1) catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. It is responsible for the primary ubiquitin-protein isopeptide bond formation and is a critical component for the initiation of in vitro conjugation reactions. UBE1 activates ubiquitin by the ATP dependent adenylation of its C-terminal glycine carboxyl group. This ubiquitin residue is then linked to the sulphydryl side chain moiety of a cysteine residue within UBE1 by forming a high-energy thiol ester bond, liberating free AMP. There are two active sites within the UBE1 molecule allowing it to accommodate two ubiquitin molecules at one time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site. The activated ubiquitin is then transferred to the lysine of target proteins via the E2/E3 conjugation cascade.

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Research area: Cell Signaling

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

Purified using immobilized metal affinity chromatography.

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