Analytical Data
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Gene name
ppa
- Application
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Alternative Names
ACP5;Tartrate-resistant acid phosphatase type 5
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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
P0A7A9
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Expression Region
1-176aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSLLNVPAGKDLPEDIYVVIEIPANADPIK YEIDKESGALFVDRFMSTAMFYPCNYGYINHTLSLDGDPVDVLVPTPYPL QPGSVIRCRPVGVLKMTDEAGEDAKLVAVPHSKLSKEYDHIKDVNDLPEL LKAQIAHFFEHYKDLEKGKWVKVEGWENAEAAKAEIVASFERAKNK
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Molecular Weight
22 kDa i
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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
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Protein Description
PPA (phosphoenolpyruvate carboxykinase) recombinant proteins have gained significant attention in the fields of biochemistry and molecular biology due to their critical role in gluconeogenesis and metabolic regulation. The enzyme PPA catalyzes the conversion of oxaloacetate to phosphoenolpyruvate, a key step in glucose synthesis from non-carbohydrate sources, which is vital for maintaining blood glucose levels during fasting or starvation conditions. Recombinant DNA technology has enabled scientists to produce PPA in various host systems, allowing for detailed study of its structure, function, and regulation. Additionally, the ability to produce PPA in a controlled and purified form opens pathways for investigations into its potential applications in metabolic engineering, therapeutic interventions, and understanding the physiological roles of gluconeogenesis in chronic diseases, such as diabetes. As researchers explore the enzyme's kinetics and interactions with other metabolic pathways, the insights gained could lead to innovative strategies for managing metabolic disorders and optimizing biotechnological processes, highlighting the importance of PPA recombinant proteins in both fundamental research and practical applications.
