Ubiquitin Activating Enzyme (UBA1), human recombinant

Catalog number: SBB-CE0011, 50 µg

UBA1 is the canonical Ubiquitin E1 activating enzyme, which catalyzes the first step of the Ubiquitin conjugation cascade. UBA1 charges Ubiquitin to a thioester on its active site cysteine through an adenylate intermediate.[1][2][3][4]

In stock


UBA1, the canonical Ubiquitin E1 activating enzyme is a 118kDa protein, which forms a homodimer in its active state. It activates Ubiquitin in an ATP-dependent mechanism where ATP is hydrolyzed to AMP and PPi, a Ubiquitin C-terminal adenylate intermediate is formed, then transferred to the E1’s active site cysteine through a thioester bond. This thioester is then transferable to an E2 conjugating enzyme’s active site cysteine. Working concentrations of this enzyme range from 10 to 100nM. This enzyme is produced recombinantly from insect cells.

For Research Use Only, Not For Use In Humans.


Product Overview
Quantity: 50 µg
Molecular Weight: 118 kDa
Purity: >95% by SDS-PAGE
Storage Buffer: 50 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 2mM TCEP
Storage Store at −80°C after product arrival. Avoid multiple freeze / thaws. It is recommended to make multiple aliquots after the first thaw.

Figures & Data

UBA1, human recombinant

Figure 1. UBA1, SDS-PAGE From left to right, increasing amounts of UBA1 loaded onto a 4-12% SDS-PAGE gel, stained with Coomassie blue.

Citations & References

1) Hershko, A., Heller, H., Elias, S., and Ciechanover, A. 1983. Components of ubiquitin–protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258: 8206–8214

2) Yang, Yili, et al. "Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics." Cancer research 67.19 (2007): 9472-9481.

3) Lee, Imsang, and Hermann Schindelin. "Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes." Cell 134.2 (2008): 268-278.

4) Olsen, Shaun K., and Christopher D. Lima. "Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer." Molecular cell 49.5 (2013): 884-896.