Analytical Data
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Gene name
PpsA
- Application
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Alternative Names
Pyruvate, water dikinase
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23538
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Expression Region
2-792aa
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Molecular Weight
103.3 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
PpsA is a key protein involved in the photosynthetic process of cyanobacteria, functioning as a phosphoenolpyruvate carboxylase (PEPC). The study of PpsA recombinant protein has gained significant attention due to its potential applications in biotechnology and bioengineering. Understanding the structure and function of PpsA can provide insights into carbon fixation pathways and improve photosynthetic efficiency in cyanobacteria, which are crucial for sustainable biofuel production and carbon sequestration. Moreover, recombinant PpsA can serve as a model for investigating enzyme kinetics, regulatory mechanisms, and metabolic engineering strategies. Recent advancements in recombinant protein technology have enabled the efficient expression and purification of PpsA, allowing researchers to explore its enzymatic properties and stability under various environmental conditions. This work not only contributes to fundamental knowledge of photosynthetic organisms but also opens avenues for utilizing PpsA in synthetic biology to enhance crop productivity and develop innovative solutions to combat climate change.
