Analytical Data
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Gene name
ATP6V0E
- Application
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Alternative Names
ATP6V0E1; ATP6H; ATP6V0E; V-type proton ATPase subunit e 1; V-ATPase subunit e 1
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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
O15342
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Expression Region
1-81aa
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AA Sequence
MAYHGLTVPLIVMSVFWGFVGFLVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP
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Molecular Weight
35.8 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
ATP6V0E, a subunit of the vacuolar H+-ATPase (V-ATPase) complex, plays a crucial role in various cellular processes, including acidification of organelles, protein sorting, and membrane trafficking. The V-ATPase complex is essential for maintaining pH homeostasis and ion balance within cells, and it is also involved in diverse physiological functions such as bone resorption, neurotransmitter release, and immune responses. Dysregulation of ATP6V0E and V-ATPase activity has been implicated in several diseases, including cancer, osteopetrosis, and metabolic disorders. Research into recombinant ATP6V0E protein has gained traction as it facilitates the study of the structure-function relationship of this subunit, its interactions within the V-ATPase complex, and its role in disease mechanisms. The production of recombinant ATP6V0E enables detailed biochemical assays, structural analyses, and potentially the development of targeted therapeutic strategies to modulate V-ATPase activity. Understanding the functional dynamics of ATP6V0E can provide insights into its regulatory mechanisms and the broader implications of V-ATPase in health and disease.
