S. cerevisiae SUMO E1 (SAE1/UBA2) (DAG2656)

S. cerevisiae SUMO E1 (SAE1/UBA2), recombinant protein from E. coli Datasheet

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Product Overview
S. cerevisiae SUMO E1 (SAE1/UBA2)
Nature
Recombinant
Tag/Conjugate
Unconjugated
Purity
> 90% by SDS-PAGE
Buffer
in 50 mM HEPES pH 8.0, 150 mM NaCl
Storage
2-8°C short term, -20°C long term
Introduction
Small Ubiquitin-like Modifier (or SUMO) proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle. SUMO proteins are similar to ubiquitin, and SUMOylation is directed by an enzymatic cascade analogous to that involved in ubiquitination. In contrast to ubiquitin, SUMO is not used to tag proteins for degradation. Mature SUMO is produced when the last four amino acids of the C-terminus have been cleaved off to allow formation of an isopeptide bond between the C-terminal glycine residue of SUMO and an acceptor lysine on the target protein. Saccharomyces cerevisiae is a species of yeast. It is perhaps the most useful yeast, having been instrumental to winemaking, baking and brewing since ancient times. It is believed that it was originally isolated from the skin of grapes (one can see the yeast as a component of the thin white film on the skins of some dark-colored fruits such as plums; it exists among the waxes of the cuticle). It is one of the most intensively studied eukaryotic model organisms in molecular and cell biology, much like Escherichia coli as the model bacterium. It is the microorganism behind the most common type of fermentation. S. cerevisiae cells are round to ovoid, 5–10 micrometres in diameter. It reproduces by a division process known as budding.
Antigen Description
Conjugation of the ubiquitin-like modifier SUMO (Sentrin) 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.
Keywords
S. cerevisiae SUMO protein; SUMO protein; Small Ubiquitin-like Modifier; SUMO; Saccharomyces cerevisiae; S. cerevisiae; Saccharomyces; Saccharomycetaceae; Saccharomyces cerevisiae Small Ubiquitin-like Modifier

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