protein

UBA5 Protein, Human (His)

HY-P71395

10 μg;50 μg

120;360 USD

UBA5 Protein, Human (His)

proteins

E. coli

10 μg;50 μg

120;360 USD

The UBA5 protein activates UFM1 in ufmylation, linking the C-terminal glycine residue of UFM1 to a cysteine residue in E1. UBA5 Protein, Human (His) is the recombinant human-derived UBA5 protein, expressed by E. coli , with N-6*His labeled tag.

Human

UBA5, functioning as an E1-like enzyme, plays a pivotal role in the initiation of ufmylation, a post-translational modification process. The activation of UFM1 begins with the adenylation of its C-terminal glycine residue by UBA5 in conjunction with ATP. This results in the formation of a UFM1-E1 thioester and free AMP. Notably, UBA5 achieves this through a trans-binding mechanism, where UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer. This trans-binding not only facilitates the stabilization of the UBA5 homodimer but also enhances ATP-binding. Subsequently, UFM1 is transferred from UBA5 to the E2-like enzyme UFC1, again employing a trans mechanism. Ufmylation, orchestrated by UBA5, emerges as a critical process involved in reticulophagy (ER-phagy) triggered by endoplasmic reticulum stress. Moreover, Ufmylation proves indispensable for the erythroid differentiation of both megakaryocytes and erythrocytes. UBA5 exists as a homodimer, and this homodimerization is essential for UFM1 activation. UBA5 also engages in specific interactions with UFM1, GABARAPL2, GABARAP, GABARAPL1, and UFC1, underscoring its intricate involvement in diverse cellular processes.

Ubiquitin-like modifier-activating enzyme 5; ThiFP1; UFM1-activating enzyme; Ubiquitin-activating enzyme E1 domain-containing protein 1; UBE1DC1; UBA5

Greater than 90% as determined by reducing SDS-PAGE.

Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT, 10% Glycerol, pH 8.0 .

Shipping with dry ice