Analytical Data
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Gene name
Atp5j
- Application
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Alternative Names
Atp5j；ATP5A；ATP5J；ATPM；ATP synthase-coupling factor 6. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18859
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Expression Region
1-108aa
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AA Sequence
NKELDPIQKLFVDKIREYKSKRQTSGGPVDASSEYQQELERELFKLKQMFGNADMNTFPTFKFEDPKFEVIEKPQA
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Molecular Weight
36.0 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
ATP5J, a gene encoding a subunit of the mitochondrial ATP synthase complex, plays a crucial role in cellular energy production through oxidative phosphorylation. This enzyme complex is vital for the synthesis of ATP, the primary energy currency of the cell. Research into ATP5J has gained momentum due to its implications in various metabolic disorders and mitochondrial dysfunctions. Mutations or dysregulation of ATP5J may lead to impaired ATP generation, contributing to conditions such as cardiomyopathy, neurodegenerative diseases, and other disorders related to energy metabolism. Additionally, since ATP5J is involved in the structural stability and function of the ATP synthase complex, studying its recombinant protein can provide insights into the biochemical pathways affected in these diseases. Investigating ATP5J could also uncover potential therapeutic targets or biomarkers for mitochondrial diseases. The development of recombinant ATP5J proteins allows for detailed structural and functional analyses, facilitating the understanding of its role in mitochondrial physiology and pathology. By elucidating the function of ATP5J and its interactions within the mitochondrial complex, researchers aim to advance our understanding of energy metabolism at the cellular level, which may lead to novel therapeutic strategies for diseases linked to mitochondrial dysfunction.
