Analytical Data
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Gene name
PLD
- Application
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Alternative Names
PLD1; Choline Phosphatase 1; Phosphatidylcholine-hydrolyzing phospholipase D1
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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
Q13393
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Expression Region
Thr725~Thr1074
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Molecular Weight
43kDa
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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
Phospholipase D (PLD) is an enzyme involved in the phospholipid metabolism that catalyzes the hydrolysis of phosphatidylcholine to produce phosphatidic acid and choline. Its role in various cellular processes, such as membrane trafficking, cell signaling, and cytoskeletal rearrangement, has sparked significant interest in the biochemical and medical research communities. Given its involvement in important physiological processes, PLD is implicated in various diseases, including cancer, cardiovascular disorders, and neurodegenerative diseases. The production of recombinant PLD proteins has become essential for studying its structure-function relationships, enzymatic mechanisms, and regulatory pathways. Generating these proteins in suitable expression systems allows researchers to perform detailed biochemical assays, kinetic analyses, and structural studies that can reveal insights into PLD's role in health and disease. Moreover, understanding PLD's function can advance therapeutic strategies targeting its pathways, providing avenues for potential drug development. The ongoing research into PLD and its recombinant forms is essential for elucidating the complex molecular interactions within cells and has the potential to unveil novel targets for intervention in various pathological conditions.
