Analytical Data
-
Gene name
aroH
- Application
-
Alternative Names
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase DAHP synthase Phospho-2-keto-3-deoxyheptonate aldolase
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P00887
-
Expression Region
1-348aa
-
Molecular Weight
42.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 study of aroH recombinant protein is rooted in the field of microbial biotechnology and metabolic engineering. AroH, a gene encoding an enzyme involved in the shikimic acid pathway, is crucial for the biosynthesis of aromatic amino acids in bacteria and plants. This pathway is essential not only for the production of key metabolites like phenylalanine, tyrosine, and tryptophan but also for the synthesis of numerous bioactive compounds, including pharmaceuticals and agrochemicals. Recently, there has been a growing interest in engineering microbial cells that can efficiently produce these compounds by optimizing the shikimic acid pathway. The successful expression and characterization of aroH recombinant protein can provide insights into enzyme function, kinetics, and regulatory mechanisms, thus facilitating the development of microbial strains with enhanced aromatic compound biosynthesis capabilities. Understanding aroH's role may also enable the development of novel strategies for bioprocess optimization, contributing to sustainable production methods in industrial biotechnology. Moreover, the incorporation of recombinant aroH into metabolic engineering frameworks could lead to the creation of microbial platforms with tailored metabolic profiles to meet various industrial needs, thereby advancing the broader application of biotechnology in food, health, and environmental sectors.
