Analytical Data
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Gene name
araA
- Application
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Alternative Names
araA；L-arabinose isomerase
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MLQTKDYEFWFVTGSQHLYGEETLELVDQHAKSICEGLSGISSRYKITHKPVVTSPETIRELLREAEYSETCAGIITWMHTFSPAKMWIEGLSSYQKPLMHLHTQYNRDIPWGTIDMDFMNSNQSAHGDREYGYINSRMGLSRKVIAGYWDDEEVKKEMSQWMDTAAALNESRHIKVARFGDNMRHVAVTDGDKVGAHIQFGWQVDGYGIGDLVEVMDRITDDEVDTLYAEYDRLYVISEETKRDEAKVASIKEQAKIELGLTAFLEQGGYTAFTTSFEVLHGMKQLPGLAVQRLMEKGYGFAGEGDWKTAALVRMMKIMAKGKRTSFMEDYTYHFEPGNEMILGSHMLEVCPTVALDQPKIEVHSLSIGGKEDPARLVFNGISGSAIQASIVDIGGRFRLVLNEVNGQEIEKDMPNLPVARVLWKPEPSLKTAAEAWILAGGAHHTCLSYELTAEQMLDWAEMAGIESVLISRDTTIHKLKHELKWNEALYRLQK
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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
AraA, an enzyme involved in the metabolism of L-arabinose, plays a pivotal role in the bacterial utilization of this five-carbon sugar. Its importance stems from the broad implications of L-arabinose as a potential renewable carbon source in biotechnology, particularly for the production of biofuels and bioplastics. In microorganisms such as *Escherichia coli*, AraA facilitates the conversion of L-arabinose into D-xylulose-5-phosphate, integrating this sugar into central metabolic pathways. The recombination and expression of araA as a recombinant protein allow researchers to study its structure and function in detail, which is essential for understanding its catalytic mechanisms and regulatory properties. Furthermore, the ability to manipulate araA through genetic engineering enables the enhancement of microbial strains for more efficient L-arabinose utilization. The characterization of AraA’s biochemical properties could also lead to applications in synthetic biology, where engineered pathways are developed for efficient sugar conversion in industrial processes. Overall, the study of araA recombinant protein not only advances fundamental microbiological research but also contributes to the sustainable use of agricultural waste and the development of environmentally friendly bioprocesses.
