Analytical Data
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Gene name
phoA
- Application
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Alternative Names
Alkaline phosphatase; phoA; Escherichia coli (strain K12); APase; Hydrolase; 3.1.3.1
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Species
E.coli
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00634
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Expression Region
M1-K471
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Protein Length
Full Length
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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 research on the PhoA recombinant protein primarily focuses on its applications in various fields such as molecular biology, biotechnology, and medicine. PhoA, or alkaline phosphatase, is an enzyme that catalyzes the hydrolysis of phosphate groups from molecules, thus playing a pivotal role in dephosphorylation processes. Its significance extends beyond basic biochemistry; PhoA is widely utilized as a reporter gene in gene expression studies, where its detectable enzymatic activity can indicate successful gene transfer and regulation. Furthermore, engineering PhoA for enhanced stability and activity holds potential for developing new biocatalysts in industrial applications. The ability to produce large quantities of active PhoA through recombinant DNA technology has opened avenues for exploring its therapeutic applications, such as in the development of enzyme replacement therapies. Additionally, understanding the structure-function relationships of PhoA through mutational analyses and crystallography is crucial for designing improved variants with tailored properties. Overall, the ongoing research into PhoA recombinant protein is essential not only for advancing basic scientific knowledge but also for harnessing its capabilities in various practical applications.
