Analytical Data
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Gene name
ATP6V1G1
- Application
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Alternative Names
V-ATPase 13KDA subunit 1Vacuolar proton pump subunit G 1Vacuolar proton pump subunit M16
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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
O75348
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Expression Region
2-118aa
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Molecular Weight
40.6 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
ATP6V1G1, a subunit of the vacuolar ATPase (V-ATPase) complex, plays a critical role in regulating intracellular pH, protein sorting, and membrane trafficking by facilitating the hydrolysis of ATP to drive proton transport across membranes. This ATP-driven proton pump is crucial for various cellular processes, including nutrient sensing, autophagy, and cell proliferation. Dysregulation or mutations in the ATP6V1G1 gene have been linked to several pathological conditions, including cancer and neurodegenerative diseases, emphasizing the importance of understanding its function and regulation. Scientists employ recombinant protein technology to produce ATP6V1G1 for detailed biochemical studies, structural analysis, and functional assays. By generating purified ATP6V1G1 in a controlled environment, researchers can investigate its interactions with other V-ATPase components, elucidate its role in cellular mechanisms, and explore potential therapeutic targets. Furthermore, understanding the dynamics of ATP6V1G1 can contribute to the development of drugs aimed at modulating V-ATPase activity, which may have implications in treating diseases associated with its dysfunction. Thus, research surrounding recombinant ATP6V1G1 is pivotal in advancing our knowledge of cellular physiology and pathology.
