Analytical Data
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Gene name
ARO
- Application
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Alternative Names
ARO；aro-2；aro-4；aro-5；Pentafunctional AROM polypeptide
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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
P11511
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Expression Region
1-218aa
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AA Sequence
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGP GYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKS SSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMK ALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSN TLFLRIPLDGTEIFTLTS
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Molecular Weight
50 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
ARO (Aromatic Amino Acids-Responsive Operon) recombinant proteins have garnered significant attention in the field of biotechnology and molecular biology due to their pivotal role in metabolic processes. These proteins are involved in the regulation of aromatic amino acid biosynthesis, which is crucial for cellular growth and development in various organisms. Understanding the structure and function of ARO proteins can provide insights into metabolic pathways and facilitate the development of biotechnological applications, such as the production of high-value aromatic compounds and pharmaceuticals. Furthermore, recent advancements in genetic engineering and protein expression systems have enabled researchers to produce ARO recombinant proteins with enhanced stability and activity. This has opened up new avenues for studying their biological functions and interactions at a molecular level, leading to potential applications in metabolic engineering and synthetic biology. The increasing interest in sustainable production methods further highlights the importance of ARO proteins, as they can serve as biocatalysts in the conversion of renewable resources into valuable chemicals. As such, the exploration of ARO recombinant proteins represents a promising area of research with implications for both fundamental science and industrial applications.
