Analytical Data
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Gene name
pdh
- Application
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Alternative Names
pdhPhenylalanine dehydrogenase; PheDH; EC 1.4.1.20
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Species
Sporosarcina ureae
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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
P97014
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Expression Region
1-379aa
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Molecular Weight
45.3 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
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Protein Description
PDH (Pyruvate Dehydrogenase) is a crucial enzyme complex in cellular metabolism, responsible for converting pyruvate into acetyl-CoA, linking glycolysis to the citric acid cycle. Its proper functioning is vital for energy production and metabolic homeostasis. Dysfunctions in PDH can lead to various metabolic disorders, including lactic acidosis and neurological diseases. Research on PDH has gained momentum due to its implications in conditions like diabetes and cancer, where altered metabolic pathways are observed. Moreover, the complex structure of PDH, comprising multiple subunits and co-factors, presents challenges for both functional studies and therapeutic interventions. Recent advances in recombinant protein technology have facilitated the production of intact and active PDH components for in vitro studies, allowing researchers to investigate its regulation and interactions at a molecular level. This has opened new avenues for understanding the role of PDH in metabolism and its potential as a therapeutic target. By exploring PDH's structural and functional properties through recombinant methodologies, scientists aim to design novel strategies to modulate its activity, with implications for treating various metabolic diseases.
