Analytical Data
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Gene name
DGKA
- Application
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Alternative Names
DGK-A; DAGK; DAGK1; DGK-alpha; 80 kDa diacylglycerol kinase; Diglyceride kinase alpha
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P51556
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Expression Region
Ala312~Glu557
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Molecular Weight
32kDa
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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
DGKA (Diacylglycerol kinase alpha) is an important enzyme that plays a crucial role in lipid metabolism and cell signaling by converting diacylglycerol (DAG) to phosphatidic acid (PA). The balance between these two lipid molecules is vital for regulating various cellular processes, including cell proliferation, differentiation, and apoptosis. Dysregulation of DGKA has been implicated in several diseases, such as cancer, cardiovascular disorders, and neurological conditions, making it a potential therapeutic target. Research on recombinantly expressed DGKA proteins is essential for understanding its structure-function relationships, mechanism of action, and interaction with other signaling molecules. Advances in recombinant DNA technology and protein expression systems have enabled the production of DGKA in various host organisms, allowing for detailed biochemical analyses and the development of high-throughput screening assays for potential DGKA inhibitors. This research not only enhances our understanding of DGKA's role in cellular signaling pathways but also paves the way for the discovery of novel therapeutics that could modulate DGKA activity and address related diseases.
