Analytical Data
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Gene name
ATP5I
- Application
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Alternative Names
ATP5K; ATPase subunit e; F1F0 ATP synthase murine e subunit; MGC12532; mitochondrial
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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
P56385
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Expression Region
1-69aa
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AA Sequence
MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARELAEDDSILK
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Molecular Weight
33.33 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
ATP5I, also known as ATP synthase subunit 5I, is a crucial component of the mitochondrial ATP synthase complex, which is essential for oxidative phosphorylation and ATP production in eukaryotic cells. Research into ATP5I has gained traction due to its potential involvement in various metabolic disorders and mitochondrial dysfunction, which are linked to a range of diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases. Recent studies have highlighted ATP5I's role not only in ATP production but also in regulating mitochondrial dynamics and cellular stress responses. Given the importance of ATP synthase in cellular energy metabolism, recombinant ATP5I proteins are being produced for structural and functional studies, aimed at elucidating its precise role in mitochondrial function and potential implications in disease pathology. Investigating this protein provides insights into the fundamental processes of energy metabolism and identifies ATP5I as a potential therapeutic target for diseases associated with mitochondrial dysfunction. Thus, the study of recombinant ATP5I is crucial for advancing our understanding of mitochondrial biology and developing novel treatment strategies.
