Analytical Data
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Gene name
aroH
- Application
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Alternative Names
aroH；C6orf150；MB21D1；Cyclic GMP-AMP synthase
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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
P00887
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Expression Region
1-348aa
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AA Sequence
MNRTDELRTARIESLVTPAELALRYPVTPGVATHVTDSRRRIEKILNGEDKRLLVIIGPCSIHDLTAAMEYATRLQSLRNQYQSRLEIVMRTYFEKPRTVVGWKGLISDPDLNGSYRVNHGLELARKLLLQVNELGVPTATEFLDMVTGQFIADLISWGAIGARTTESQIHREMASALSCPVGFKNGTDGNTRIAVDAIRAARASHMFLSPDKNGQMTIYQTSGNPYGHIIMRGGKKPNYHADDIAAACDTLHEFDLPEHLVVDFSHGNCQKQHRRQLEVCEDICQQIRNGSTAIAGIMAESFLREGTQKIVGSQPLTYGQSITDPCLGWEDTERLVEKLASAVDTRF
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Molecular Weight
42.8 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 aroH gene, encoding a key enzyme for the tryptophan biosynthetic pathway, has garnered significant attention in microbial biotechnology and metabolic engineering. This gene is primarily found in bacteria and plays a crucial role in the conversion of chorismate to anthranilate, the precursor for tryptophan synthesis. The manipulation of aroH expression is of particular interest due to its implications in enhancing the production of various aromatic compounds, which have applications in pharmaceuticals, flavorings, and fragrances. Research has shown that by overexpressing aroH, bacterial strains can be engineered to improve their yield of tryptophan and its derivatives, thus facilitating the development of more efficient bioprocesses. Additionally, the aroH gene has been implicated in microbial resistance mechanisms and can influence pathogenicity in certain bacterial species. Therefore, understanding the structure, function, and regulation of the aroH gene is essential for advancing genetic engineering approaches aimed at optimizing aromatic compound production while also providing insights into bacterial metabolism and adaptation. Recent advances in synthetic biology and CRISPR technologies have further propelled the exploration of aroH, allowing for precise modifications and the potential development of robust microbial platforms for bioproduction. The ongoing research not only aims to enhance yield and efficiency but also to explore the ecological and evolutionary significance of the aroH pathway in diverse microbial communities.
