Product Details
| MW: | ~38kDa and 90kDa |
| |
| Source: | Produced in E. coli. Full length heterodimeric human SUMO-activating enzyme. |
| |
| UniProt ID: | Q9UBE0 (subunit 1), O95605 (subunit 2) |
| |
| Formulation: | Liquid. In 20mM HEPES, pH 8.0, containing 110mM potassium acetate, 2mM magnesium acetate, 0.5mM EGTA and 1mM DTT. |
| |
| Shipping: | Dry Ice |
| |
| Long Term Storage: | -80°C |
| |
| Scientific Background: | SUMO conjugation to target proteins is mediated by a different, but analogous, pathway to ubiquitinylation. SUMO activating enzyme is a heterodimeric complex consisting of Aos1 and Uba2. Both subunits are well conserved from yeast to humans, with Aos2/SAE I being similar to the N-terminal half of the E1 enzyme for ubiquitin while Uba2/SAE II has similarity to the C-terminal half, and contains the active site cysteine residue required for formation of thioester bonds. However, Uba2 alone is not sufficient to catalyze SUMOylation. SUMO1 activating enzyme supports in vitro SUMOylation. |
| |
| Regulatory Status: | RUO - Research Use Only |
| |
SUMOylation assay utilising SUMO-1, SUMO E1 (Prod. No. BML-UW9330), SUMO E2 (Prod. No. BML-UW9320) and RanGAP1 as target protein in presence (lane 2) and absence (lanes (1) of ATP after SDS-PAGE and blotting to PVDF with subsequent probing with Prod. No. BML-PW9460 (Anti-SUMO1).
SUMO E1 heterodimer by SDS-PAGE. Lane M: Markers, in kDa (from top to bottom), 205, 116, 97, 84, 66, 55, 45 and 36; Lane 1: SUMO E1 heterodimer, final product solution.
Please mouse over
Product Literature References
DEK oncoprotein participates in heterochromatin replication via SUMO-dependent nuclear bodies: A. Pierzynska-Mach, et al.; J. Cell Sci. (2023),
Abstract;
Tricyclic antidepressants target FKBP51 SUMOylation to restore glucocorticoid receptor activity: M.L. Budziñski, et al.; Mol. Psychiatry
27, 2533 (2022),
Abstract;
Detection and Analysis of SUMOylation Substrates In Vitro and In Vivo: C. Cedeno, et al.; Methods Mol. Biol.
1449, 267 (2016),
Abstract;
hnRNP K coordinates transcriptional silencing by SETDB1 in embryonic stem cells: P.J. Thompson, et al.; PLoS Genet.
11, e1004933 (2015),
Abstract;
Full Text
