Recombinant Yeast GST-SUMO E1 (SAE1/UBA2) Protein, CF
Recombinant Yeast GST-SUMO E1 (SAE1/UBA2) Protein, CF Summary
Contains an N-terminal GST (glutathione S-transferase) tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|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 requires the activities of the heterodimeric E1 (Aos1/Uba2) and the UbcH9 E2 enzyme. The dimeric activating enzyme utilizes ATP to adenylate the C-terminal glycine residue of SUMO-1 (also SUMO-2 and SUMO-3), forming a high-energy thiolester bond with the cysteine residue of Uba2 and the release of AMP and PPi. The second step is the trans-esterification reaction whereby SUMO-1 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.
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