Analytical Data
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Gene name
ATP5MG
- Application
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Alternative Names
ATP synthase membrane subunit g (ATPase subunit g) (ATP5L)
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Species
Bovine
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q28852
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Expression Region
2-103aa
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Molecular Weight
18.7 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
ATP5MG is an essential component of the mitochondrial ATP synthase complex, playing a crucial role in energy production through oxidative phosphorylation. This protein is encoded by the ATP5MG gene, which is located within the mitochondrial DNA. Research on ATP5MG has gained momentum due to its implications in various metabolic disorders and mitochondrial diseases, which are often characterized by dysfunction in energy production. Studies have shown that mutations or dysregulation of ATP5MG can lead to impaired mitochondrial function, resulting in conditions such as myopathies, neurodegenerative diseases, and other metabolic syndromes. The recombinant expression of ATP5MG provides a valuable tool for understanding its structure, function, and interactions within the ATP synthase complex. By characterizing the protein through various biochemical and biophysical techniques, researchers aim to elucidate its role in mitochondrial bioenergetics and its potential as a therapeutic target. Additionally, understanding the mechanisms by which ATP5MG contributes to ATP synthesis and how its dysfunction affects cellular metabolism may open new avenues for the development of treatments for mitochondrial-related diseases. Overall, the study of recombinant ATP5MG not only enhances our knowledge of mitochondrial biology but also highlights the importance of this protein in maintaining cellular energy homeostasis.
