SAE1/SAE2 Human
Sf9 insect cells.
Greater than 95.0% as determined by SDS-PAGE.
Description
SAE1/SAE2 Human Recombinant produced in SF9 is glycosylated, polypeptide chain containing 2 subunits (SAE1 subunit molecular mass is 41kDa & SAE2 subunit molecular mass is 91kDa). The subunits associate to form a complex.
The SAE1/SAE2 is expressed with a -10xHis tag and purified by proprietary chromatographic techniques.
Product Specs
SAE1 and SAE2 proteins combine to form heterodimers, which are involved in sumoylation, a protein modification process. Sumoylation is crucial for regulating protein structure and determining their location within cells. The presence of autoantibodies against SAE1/SAE2 in patients suggests their potential as biomarkers for dermatomyositis (DM).
Recombinant human SAE1/SAE2, produced in SF9 insect cells, is a glycosylated polypeptide chain comprising two subunits. The SAE1 subunit has a molecular mass of 41 kDa, while the SAE2 subunit has a molecular mass of 91 kDa. These subunits assemble to form a functional complex. The SAE1/SAE2 complex is expressed with a 10xHis tag to facilitate purification, which is achieved using proprietary chromatographic methods.
The SAE1/SAE2 protein is supplied in a buffer containing 20mM HEPES (pH 8.0), 200mM NaCl, and 20% glycerol.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to freeze the product at -20°C. Repeated freezing and thawing should be avoided to maintain product integrity.
The purity of the SAE1/SAE2 protein is greater than 95%, as determined by SDS-PAGE analysis.
1. The SAE1/SAE2 protein specifically binds to human autoantibodies of the IgG class.
2. This protein serves as a valuable reagent in standard ELISA tests, enabling checkerboard analysis of positive and negative samples, as well as in immunodot assays for qualitative detection of positive and negative samples.
The SAE1/SAE2 protein is suitable for Western blot analysis, particularly for detecting the presence of anti-SAE1/SAE2 autoantibodies in positive samples. It can be used in conjunction with polyclonal antibodies against SAE1 and SAE2.
The recommended coating concentration for ELISA is 0.3-0.8 µg/ml, which may vary depending on the specific ELISA plate type and coating buffer used. The SAE1/SAE2 protein is suitable for conjugation to various functional groups.
Sf9 insect cells.
Product Science Overview
SAE1/SAE2, also known as SUMO-activating enzyme subunit 1 and subunit 2, respectively, are crucial components in the SUMOylation pathway. SUMOylation is a post-translational modification process that involves the attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target proteins, influencing their function, localization, and stability. The SAE1/SAE2 heterodimer acts as an E1 enzyme, initiating the SUMOylation process by activating SUMO proteins in an ATP-dependent manner .
The SAE1/SAE2 complex is composed of two subunits: SAE1 and SAE2. SAE1, also known as AOS1, and SAE2, also known as UBA2, form a heterodimer that is essential for the activation of SUMO proteins. The activation process involves the formation of a thioester bond between the catalytic cysteine residue of SAE2 and the SUMO protein .
The SAE1/SAE2 complex is responsible for the first step in the SUMOylation cascade, which includes:
SUMOylation plays a vital role in various cellular processes, including DNA repair, transcriptional regulation, and signal transduction. Dysregulation of SUMOylation has been implicated in several diseases, including cancer, neurodegenerative disorders, and viral infections .
SAE1/SAE2 is indispensable for protein SUMOylation, and its dysregulation has been associated with the progression of various human cancers. For instance, overexpression of SAE1 has been linked to the progression of glioma, a type of brain cancer, by enhancing the SUMOylation-mediated signaling pathway .
