Analytical Data
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Gene name
PDK2
- Application
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Alternative Names
PDHK2; [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial
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Species
Mouse
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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
Q9JK42
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Expression Region
Leu155~Trp380
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Molecular Weight
29kDa
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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
PDK2 (Pyruvate Dehydrogenase Kinase 2) is a critical enzyme involved in the regulation of cellular metabolism, specifically in the control of the pyruvate dehydrogenase complex, which plays a pivotal role in converting pyruvate into acetyl-CoA, linking glycolysis to the tricarboxylic acid (TCA) cycle. The dysregulation of PDK2 and its associated pathways has been implicated in various metabolic disorders, including obesity, diabetes, and cancer. Due to its significant role in altering glucose metabolism and promoting a glycolytic phenotype in tumors, PDK2 has garnered attention as a potential therapeutic target. The recombinant expression of PDK2 has allowed researchers to investigate its structural and functional properties, providing insights into its catalytic mechanisms and regulatory interactions. Furthermore, understanding the modulation of PDK2 activity can uncover novel approaches for interventions in metabolic diseases. The development of specific PDK2 inhibitors might not only enhance metabolic homeostasis but also offer strategies for cancer treatment by disrupting the metabolic flexibility of tumor cells. Thus, the study of recombinant PDK2 not only facilitates a deeper understanding of its biological function but also holds promise for advancing therapeutic avenues in metabolic and oncological research.
