>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
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.
E. coli-derived human SUMO Activating Enzyme E1 (SAE1/UBA2) protein
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.
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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.
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