Recombinant Human SUMO E1 (SAE1/UBA2) Protein, CF
Recombinant Human SUMO E1 (SAE1/UBA2) Protein, CF Summary
|Formulation||Supplied as a solution in HEPES, NaCl, DTT and Glycerol.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: SUMO Activating Enzyme E1 (SAE1/UBA2)
Small Ubiquitin-like Modifier (SUMO) Activating Enzyme Subunit 1 (SAE1) is the highly conserved human ortholog of yeast Ubiquitin-activating enzyme E1-like (UBA2) (1). These SUMO-activating (E1) enzymes are critical for the enzymatic attachment of SUMO molecules to a target protein by a post-translational modification process termed SUMOylation (2-4). The ATP-dependent E1 enzyme charges the SUMO by forming a high-energy thiol ester intermediate which is transferred to the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme (5,6). The second step is the trans-esterification reaction whereby SUMO is transferred to Cys93 of UbcH9. UBE2I/Ubc9 is the only known E2 that is able to mediate the conjugation of SUMO to lysine residues on a variety of cellular targets, usually in the absence of a Ubiquitin ligase (E3). Although UBE2I/Ubc9 can directly recognize and modify lysine residues contained in a SUMOylation motif, E3-like factors most likely facilitate the SUMOylation of specific substrates.
Conjugation of the ubiquitin-like modifier SUMO (Sentrin) requires the activities of the heterodimeric E1 (SAE1/UBA2) and the UbcH9 E2 enzyme. The dimeric activating enzyme utilizes ATP to adenylate the C-terminal glycine residue of all SUMO proteins, forming a high energy thiolester bond with the cysteine residue of UBA2 and the concomitant release of AMP and PPi. The second step is the trans-esterification reaction whereby SUMO is transferred to Cys93 of UbcH9.
- Johnson, E.S. et al. (1997) EMBO J. 16:5509.
- Desterro, J.M. et al. (1997) FEBs. Lett. 417:297.
- Bettermann, K. et al. (2012) Cancer Lett. 316:113.
- Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
- Okuma, T. et al. (1999) Biochem. Biophys. Res. Commun. 254:693.
- Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
Citations for Recombinant Human SUMO E1 (SAE1/UBA2) Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 4
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Dynamic SUMO remodeling drives a series of critical events during the meiotic divisions in Caenorhabditis elegans
Authors: AC Davis-Roca, NS Divekar, RK Ng, SM Wignall
PLoS Genet., 2018;14(9):e1007626.
Species: Nematode (C. elegans)
Sample Types: Cell Lysates
Sumoylation in p27kip1 via RanBP2 promotes cancer cell growth in cholangiocarcinoma cell line QBC939
Authors: J Yang, Y Liu, B Wang, H Lan, Y Liu, F Chen, J Zhang, J Luo
BMC Mol. Biol., 2017;18(1):23.
Sample Types: Proteins
HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells
Authors: WF Wang, L Yan, Z Liu, LX Liu, J Lin, ZY Liu, XP Chen, W Zhang, ZZ Xu, T Shi, JM Li, YL Zhao, G Meng, Y Xia, JY Li, J Zhu
Nat Commun, 2017;8(1):363.
The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1? sumoylation and poly-SUMO chain elongation
Proc Natl Acad Sci USA, 2016;113(24):6725-30.
Sample Types: Recombinant Protein
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