Recombinant Human SUMO E1 (SAE1/UBA2) Protein, CF

  (3 citations)     
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Citations (3)
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  • Purity
    >90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
  • Activity
    Recombinant Human SUMO E1 (SAE1/UBA2) is a member of the SUMO-activating (E1) enzyme family that is required for the first step of the enzymatic cascade that subsequently utilizes a SUMO-conjugating (E2) enzyme to conjugate SUMO to substrate proteins. A SUMO ligase (E3) is sometimes utilized for SUMO conjugation, but is not always required. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human SUMO E1 (SAE1/UBA2) concentration of 50-500 nM.
  • Source
    E. coli-derived human SUMO Activating Enzyme E1 (SAE1/UBA2) protein
  • Accession #
  • Predicted Molecular Mass
    38 kDa (SAE1) & 71 kDa (UBA2)
Product Datasheets

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E-315
 
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.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
 
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.

  • References:
    1. Johnson, E.S. et al. (1997) EMBO J. 16:5509.
    2. Desterro, J.M. et al. (1997) FEBs. Lett. 417:297.
    3. Bettermann, K. et al. (2012) Cancer Lett. 316:113.
    4. Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
    5. Okuma, T. et al. (1999) Biochem. Biophys. Res. Commun. 254:693.
    6. Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
  • Long Name:
    SUMO1 Activating Enzyme E1
  • Entrez Gene IDs:
    10055 (Human); 56459 (Mouse); 308384 (Rat); 856310 (Yeast)
  • Alternate Names:
    AOS1; AOS1activator of SUMO1; FLJ3091; HSPC140; SAE1; SUA1; SUA1sentrin/SUMO-activating protein AOS1; SUMO Activating Enzyme E1 (SAE1/UBA2); SUMO-1 activating enzyme E1 N subunit; SUMO1 activating enzyme subunit 1; SUMO-1 activating enzyme subunit 1; SUMO-activating enzyme subunit 1; UBA2; Ubiquitin-like 1-activating enzyme E1A; ubiquitin-like protein SUMO-1 activating enzyme; UBLE1A
Related Research Areas
Citations:

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.

3 Citations: Showing 1 - 3
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Species
Applications
Sample Type
  1. 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.
    Application: Bioassay
  2. 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.
    Species: N/A
    Sample Type: Proteins
    Application: Bioassay
  3. 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.
    Species: Human
    Sample Type: Recombinant Protein
    Application: Bioassay

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