Analytical Data
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Gene name
aroA
- Application
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Alternative Names
aroA；3-phosphoshikimate 1-carboxyvinyltransferase
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Species
Human
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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
P0A6D4
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Expression Region
1-427aa
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AA Sequence
MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQAA
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Molecular Weight
53.5 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 aroA gene encodes an enzyme crucial for the shikimic acid pathway, which is essential for the biosynthesis of aromatic amino acids in many bacteria, fungi, and plants. This pathway is absent in animals, making aroA a potential target for developing antibiotics and herbicides. Research on aroA recombinant proteins has gained momentum due to their importance in metabolic engineering and biotechnology. By manipulating the aroA gene, researchers can produce modified strains with enhanced capabilities for synthesizing valuable compounds, such as pharmaceuticals and biofuels. Furthermore, the study of aroA proteins can provide insights into resistance mechanisms in bacterial pathogens, offering new avenues for therapeutic intervention. Advances in molecular cloning and expression systems have facilitated the production of recombinant aroA proteins, enabling a deeper understanding of their function and structure. This research not only contributes to fundamental microbiology but also holds promise for practical applications in agriculture and medicine. Overall, the exploration of aroA recombinant proteins continues to unravel the complexities of microbial metabolism and offers potential solutions to pressing challenges in health and food security.
