SAE1 / Unconjugated / Polyclonal
Product Details
Description | SUMO E1 activating enzyme (also called Ubiquitin-like 1 activating enzyme E1A, UBLE1A, AOS1, SAE1, and SUA1) with SAE2 (also known as UBA2) forms a heterodimeric (SAE1/SAE2) enzyme that activates the ubiquitin-like SUMO proteins (SUMO stands for Small Ubiquitin-like MOdifier.) The SAE1 (SUMO Activating Enzyme 1) subunit resembles the N-terminal half of yeast UBA1; the SAE2 (also called Uba2) subunit corresponds to the C-terminal part of yeast UBA1 and contains the active site cysteine. In the SUMO activation step, SAE1/SAE2 uses ATP to adenylate the C-terminal glycine of SUMO-1 (the first of the three different mammalian SUMO proteins) then forms a high-energy thioester bond between the C-terminal glycine and the active site cysteine in SAE2 (Uba2). In the conjugation step, the SUMO moiety is transferred from SAE1/SAE2 to the active site cysteine (Cys 93) of the SUMO conjugating enzyme (SUMO E2, Ubc9) forming a SUMO-E2 thioester complex. | |
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Conjugate | Unconjugated | |
Clone | Polyclonal | |
Target Species | Bovine, Canine, Human, Mouse, Rat | |
Applications | ELISA, WB | |
Supplier | Aviva Systems Biology | |
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About SAE1
Posttranslational modification of proteins by the addition of the small protein SUMO (see SUMO1; MIM 601912), or sumoylation, regulates protein structure and intracellular localization. SAE1 and UBA2 (MIM 613295) form a heterodimer that functions as a SUMO-activating enzyme for the sumoylation of proteins (Okuma et al., 1999 [PubMed 9920803]).[supplied by OMIM, Mar 2010]
Posttranslational modification of proteins by the addition of the small protein SUMO (see SUMO1; MIM 601912), or sumoylation, regulates protein structure and intracellular localization. SAE1 and UBA2 (MIM 613295) form a heterodimer that functions as a SUMO-activating enzyme for the sumoylation of proteins (Okuma et al., 1999 [PubMed 9920803]).[supplied by OMIM, Mar 2010]
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