Analytical Data
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Gene name
araA
- Application
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Species
strain 168
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P94523
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Expression Region
1-496aa
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Molecular Weight
63.6 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
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Protein Description
The study of araA recombinant protein is rooted in the understanding of the arabinose operon, which plays a critical role in the metabolism of the sugar L-arabinose in various microorganisms, particularly Escherichia coli. AraA is one of the key enzymes encoded by this operon, specifically responsible for catalyzing the conversion of L-arabinose to L-ribulose. Research into araA recombinant protein has gained significance due to its potential applications in biotechnology, including biofuel production and carbohydrate metabolism studies. The ability to express and purify araA in a recombinant system allows for detailed kinetic studies and structural analyses, providing insights into its enzymatic mechanisms and substrate interactions. Furthermore, understanding the regulation and functionality of araA can enhance metabolic engineering efforts aimed at optimizing microbial strains for the efficient utilization of pentose sugars derived from lignocellulosic biomass. Overall, the exploration of araA and its recombinant variants is not only vital for deciphering fundamental biological processes but also for developing innovative biotechnological solutions to address renewable energy challenges and improve bioprocesses in industrial applications.
