Analytical Data
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Gene name
ATPAF2
- Application
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Alternative Names
ATP12 homolog
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N5M1
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Expression Region
41-289aa
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Molecular Weight
32.5 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
ATPAF2 (ATP synthase assembly factor 2) is a critical protein involved in the assembly and stability of mitochondrial ATP synthase, the enzyme responsible for ATP production through oxidative phosphorylation. Dysfunction of ATP synthase can lead to a variety of mitochondrial diseases and has been implicated in age-related degenerative disorders, making ATPAF2 a significant focus of research in cellular bioenergetics. It was first identified as a key player in the assembly of ATP synthase, highlighting its essential role in maintaining proper mitochondrial function. Studies have demonstrated that ATPAF2 interacts with several mitochondrial proteins, influencing the assembly and activity of ATP synthase complexes. Given its pivotal role in energy metabolism, understanding the precise function and regulation of ATPAF2 is crucial for elucidating the mechanisms underlying mitochondrial diseases. Recent research efforts aim to explore the therapeutic potential of modulating ATPAF2 activity or its pathways to develop novel treatments for mitochondrial-related disorders. By dissecting the molecular mechanisms by which ATPAF2 aids in ATP synthase assembly, researchers hope to uncover targets for drug development, ultimately seeking to mitigate the impact of mitochondrial dysfunction on human health.
