Analytical Data
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Gene name
ATP6V1E2
- Application
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Alternative Names
ATP6V1E2; ATPase. H+ transporting. lysosomal 31kDa. V1 subunit E2
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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
Q96A05
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Expression Region
1-226aa
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AA Sequence
MALSDVDVKKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKILMSTMRNQARLKVLRARNDLISDLLSEAKLRLSRIVEDPEVYQGLLDKLVLQGLLRLLEPVMIVRCRPQDLLLVEAAVQKAIPEYMTISQKHVEVQIDKEAYLAVNAAGGVEVYSGNQRIKVSNTLESRLDLSAKQKMPEIRMALFGANTNRKFFI
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Molecular Weight
52.5 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
ATP6V1E2, a vital component of the vacuolar ATPase (V-ATPase) complex, plays a crucial role in cellular processes such as pH regulation, protein sorting, and nutrient transport. This ATPase is involved in various cellular compartments, including endosomes and lysosomes, where it drives the acidification crucial for enzyme activity and metabolic functions. Research has shown that alterations in ATP6V1E2 expression and function are linked to several diseases, including cancer and neurodegenerative disorders, making it a potential biomarker and therapeutic target. Understanding the structure and function of recombinant ATP6V1E2 can provide insights into the V-ATPase mechanism and its regulatory functions in health and disease. Advancements in recombinant protein technology have enabled the production of ATP6V1E2 for biochemical and biophysical studies, facilitating the exploration of its role in cellular homeostasis and pathology. By elucidating the functional properties and interactions of ATP6V1E2, researchers aim to uncover novel therapeutic strategies that may enhance or restore normal V-ATPase activity in disease contexts.
