Analytical Data
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Gene name
PPA1
- Application
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Alternative Names
(Pyrophosphate phospho-hydrolase)(PPase)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15181
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Expression Region
228-289aa
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Molecular Weight
10.8 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
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Protein Description
PPA1, or phosphatase PPA1, is an essential protein that plays a crucial role in cellular phosphate metabolism, particularly in the context of mitochondrial function and energy production. Research into PPA1 has gained traction due to its involvement in various physiological processes and diseases, including potential links to metabolic disorders and mitochondrial dysfunction. The enzyme is responsible for dephosphorylating inorganic pyrophosphate (PPi), thereby influencing ATP synthesis and overall cellular energy balance. Dysfunction in PPA1 has been associated with compromised mitochondrial efficiency, which can lead to various health complications. Recent studies have focused on the recombinant expression of PPA1 in heterologous systems, allowing for detailed characterization of its biochemical properties and regulation. By generating recombinant PPA1, researchers seek to elucidate its structure-function relationships and interaction with other metabolic pathways. Furthermore, the availability of purified PPA1 opens avenues for the investigation of therapeutic targets in diseases where energy metabolism is disrupted. Understanding the role of PPA1 in cellular processes not only enhances our knowledge of basic biology but also has potential implications for designing interventions in metabolic diseases, thus emphasizing the importance of this protein in both health and disease contexts. Overall, the study of PPA1 and its recombinant forms represents a significant step forward in biochemistry and molecular biology, with the potential to provide insights that may translate into clinical relevance.
