SAE2, UBA-2, SAE-2, SUMO-1 Activating Enzyme Subunit 2.
UBA2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 649 amino acids (1-640a.a) and having a molecular mass of 72.3kDa. UBA2 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
SAE2, UBA-2, SAE-2, SUMO-1 Activating Enzyme Subunit 2.
Ubiquitin-Like Modifier Activating Enzyme 2 (UBA2), also known as SUMO-activating enzyme subunit 2 (SAE2), is a crucial component in the post-translational modification process known as SUMOylation. This process involves the attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target proteins, influencing various cellular functions such as signal transduction, gene expression, and protein stability.
The concept of ubiquitin-like protein modification was first characterized in the early 1980s. UBA2 was initially identified during the characterization of E1 enzymatic activity in wheat. Human UBA2, which contains 640 amino acid residues, shares a high degree of sequence identity with SAE1, despite the latter being only 346 amino acids long. Together, these proteins form a functional heterodimeric enzyme that activates SUMO proteins in a manner analogous to the single E1 ubiquitin-activating enzymes in yeast .
UBA2 is a subunit of the E1-activating enzyme involved in the SUMOylation of numerous proteins. It forms a heterodimer with SAE1, and this complex is responsible for the ATP-dependent activation of SUMO proteins. The activated SUMO is then transferred to a conjugating enzyme (E2), which, with the assistance of an E3 ligase, attaches the SUMO to the target protein .
SUMOylation plays a vital role in various cellular processes, including cell cycle control, apoptosis, cell differentiation, and the stress response. UBA2, as part of the SUMO-activating enzyme, is essential for these processes. The modification of proteins by SUMO can alter their structure, localization, and interaction with other proteins, thereby regulating their function .
UBA2 has been implicated in the progression of various cancers. For instance, it has been observed that UBA2 is overexpressed in glioma tissues and cell lines. High expression levels of UBA2 are associated with poorer survival rates in glioma patients. Additionally, UBA2 expression correlates with drug sensitivity in cancers, making it a potential therapeutic target .