treS Protein, Thermus thermophilus

The treS protein plays a key role in carbohydrate metabolism by catalyzing the reversible interconversion of maltose and α,α-trehalose via transglucosylation. This enzyme activity is critical for the dynamic regulation of intracellular sugar utilization and storage. treS Protein, Thermus thermophilus is the recombinant treS protein, expressed by E. coli , with tag free. The total length of treS Protein, Thermus thermophilus is 963 a.a., .

The treS protein is an enzyme that plays a crucial role in carbohydrate metabolism by catalyzing the reversible interconversion of maltose and alpha,alpha-trehalose through transglucosylation. This enzymatic activity is involved in the biosynthesis and breakdown of trehalose, a disaccharide composed of two glucose molecules linked by an alpha-1,1-glycosidic bond. Trehalose serves as a versatile and protective sugar in various organisms, playing roles in stress response, energy storage, and cellular protection. The reversible action of treS facilitates the dynamic regulation of trehalose levels based on cellular requirements. Understanding the functions of treS provides insights into the intricate network of carbohydrate metabolism and the versatile roles of trehalose in cellular processes.

Others

E. coli

Tag Free

O06458 (M1-A963)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.