Analytical Data
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Gene name
treS
- Application
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Alternative Names
Trehalose synthase/amylase TreS; Maltose alpha-D-glucosyltransferase; MTase; treS; Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); Glycosidase; Hydrolase; Isomerase; 3.2.1.1
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WQ19
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Expression Region
M1-L601
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Protein Length
Full Length
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The treS gene encodes a trehalose synthase, an enzyme involved in the biosynthesis of trehalose, a disaccharide that serves as a protective osmoprotectant and energy source for many organisms, particularly in response to stress conditions such as dehydration and high salinity. Trehalose plays a crucial role in cellular protection by stabilizing proteins and cell membranes, thereby enhancing survival in extreme environments. Research on treS recombinant protein has gained attention due to its potential applications in biotechnology and agriculture, especially in developing stress-resistant crops. Furthermore, trehalose is also implicated in various physiological processes, including regulating metabolism and promoting longevity, making treS a valuable target for genetic engineering efforts aimed at enhancing crop resilience and yield. Understanding the structure and function of treS, along with its enzymatic mechanisms, could lead to innovative strategies to optimize trehalose production, thereby improving plant stress tolerance and agricultural productivity in the face of climate change and resource scarcity. As such, investigations into the recombinant expression of treS not only contribute to fundamental science but also hold promise for practical applications in sustainable agriculture and food security.
