Analytical Data
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Gene name
ATP6V0D1
- Application
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Alternative Names
32KDA accessory protein V-ATPase 40KDA accessory protein V-ATPase AC39 subunit
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61421
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Expression Region
1-351aa
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Molecular Weight
67.3 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
ATP6V0D1, a crucial subunit of the vacuolar H+-ATPase (V-ATPase) complex, plays a significant role in cellular processes, particularly in acidifying intracellular compartments and regulating various physiological functions. V-ATPases are multi-subunit enzymes responsible for transporting protons across membranes, thereby affecting pH levels and ion homeostasis within cells. Perturbations in ATP6V0D1 expression or function have been linked to several pathophysiological conditions, including cancer, neurodegenerative diseases, and metabolic disorders. Emerging research indicates that ATP6V0D1 may influence the migration and invasion of cancer cells, making it a potential target for therapeutic interventions. The ability to produce recombinant ATP6V0D1 protein is crucial for investigating its structural properties, enzymatic functions, and interactions with other cellular partners. This research not only enhances our understanding of ATP6V0D1’s role in normal physiology but also underscores its potential implications in disease contexts, paving the way for novel treatment strategies.
