Analytical Data
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Gene name
ATP6V1F
- Application
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Alternative Names
V-ATPase 14KDA subunitVacuolar proton pump subunit F
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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
Q16864
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Expression Region
1-119aa
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Molecular Weight
40.4 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
The ATP6V1F protein, a subunit of the vacuolar ATPase (V-ATPase) complex, plays a crucial role in cellular processes such as pH regulation, ion transport, and organic nutrient degradation. V-ATPase is a multi-subunit enzyme complex found in various cellular organelles, including lysosomes, endosomes, and the plasma membrane, where it is responsible for acidifying these compartments. The ATP6V1F subunit is essential for the functional integrity and assembly of the V-ATPase complex, influencing its enzymatic activity and cellular localization. Research into ATP6V1F has gained importance due to its implications in various diseases, including cancer and neurodegenerative disorders, where alterations in V-ATPase function can affect cellular homeostasis and tumor progression. Moreover, ATP6V1F expression levels and activity have been associated with the invasive potential of certain cancer cells, making it a potential target for therapeutic interventions. Understanding the structure and function of ATP6V1F through recombinant protein studies can provide insights into its role in cellular physiology and pathology, paving the way for the development of novel treatments aimed at modulating V-ATPase activity in disease contexts.
