Analytical Data
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Gene name
tktA
- Application
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Alternative Names
tktA; tkt; b2935; JW5478; Transketolase 1; TK 1; EC 2.2.1.1
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27302
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Expression Region
1-663aa
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Molecular Weight
88.2 kDa
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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 TktA protein, also known as transketolase A, is an important enzyme involved in the pentose phosphate pathway, a crucial metabolic pathway in many organisms, including bacteria and plants. This pathway plays a vital role in generating NADPH and ribose-5-phosphate, which are essential for biosynthesis and cellular redox balance. Research on TktA has gained attention due to its potential applications in biotechnology and medicine. For instance, the manipulation of this enzyme could enhance the production of valuable metabolites, such as aromatic compounds and biofuels, through metabolic engineering. Furthermore, understanding the structure-function relationship of TktA can provide insights into its catalytic mechanism and regulation, offering opportunities for the development of inhibitors that could have therapeutic implications in diseases where metabolic pathways are dysregulated. Studies have focused on the recombinant expression, purification, and characterization of TktA, utilizing various expression systems like E. coli. The introduction of site-directed mutagenesis has also enabled researchers to investigate the impact of specific amino acid residues on enzyme activity and stability. Overall, the exploration of TktA as a recombinant protein not only contributes to our fundamental understanding of metabolic processes but also holds significant promise for industrial applications and the development of novel therapeutic strategies.











