Analytical Data
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Gene name
ATP6V1G3
- Application
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Alternative Names
ATP6G3; atp6v1g3; ATPase. H+ transporting. lysosomal (vacuolar proton pump) subunit G3
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96LB4
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Expression Region
1-118aa
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AA Sequence
MTSQSQGIHQ LLQAEKRAKD KLEEAKKRKG KRLKQAKEEA MVEIDQYRMQ RDKEFRLKQS KIMGSQNNLS DEIEEQTLGK IQELNGHYNK YMESVMNQLL SMVCDMKPEI HVNYRATN
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Molecular Weight
13.9 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
ATP6V1G3, a subunit of the vacuolar ATPase (V-ATPase) complex, plays a crucial role in cellular processes by facilitating proton transport across cellular membranes. This complex is essential for maintaining intracellular pH, enabling nutrient uptake, and regulating hormone secretion. Research into ATP6V1G3 has gained momentum due to its involvement in various diseases, including cancer and neurodegenerative disorders, where dysregulation of V-ATPase activity has been observed. Recombinant protein technology allows for the expression and purification of ATP6V1G3, enabling detailed studies of its structure and function. Understanding the mechanisms by which ATP6V1G3 contributes to cellular homeostasis and its potential as a therapeutic target could provide insights into novel treatment strategies. Additionally, examining its interactions with other V-ATPase subunits and cellular components is vital for deciphering the complex regulatory networks that govern cellular metabolism and survival. As a result, ATP6V1G3 serves as an important focus in cellular biology and medical research, with the potential to unveil new avenues for therapeutic interventions in diseases associated with V-ATPase dysfunction.
