Analytical Data
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Gene name
ATPAF1
- Application
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Alternative Names
ATP synthase mitochondrial F1 complex assembly factor 1; ATP11; ATP11 homolog
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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
Q5TC12
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Expression Region
1-328aa
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AA Sequence
MAAVVVAAAGGAGPAVLQVAGLYRGLCAVRSRALGLGLVSPAQLRVFPVRPGSGRPEGGADGSGVGAEAELQANPFYDRYRDKIQLLRRSDPAAFESRLEKRSEFRKQPVGHSRQGDFIKCVEQKTDALGKQSVNRGFTKDKTLSSIFNIEMVKEKTAEEIKQIWQQYFAAKDTVYAVIPAEKFDLIWNRAQSCPTFLCALPRREGYEFFVGQWTGTELHFTALINIQTRGEAAASQLILYHYPELKEEKGIVLMTAEMDSTFLNVAEAQCIANQVQLFYATDRKETYGLVETFNLRPNEFKYMSVIAELEQSGLGAELKCAQNQNKT
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Molecular Weight
62.8 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
ATPAF1, or ATP synthase-coupling factor 1, is a crucial protein involved in mitochondrial bioenergetics, specifically in the regulation of ATP synthase activity. Research into ATPAF1 has gained momentum due to its significant role in energy metabolism and its potential implications in various diseases, including neurodegenerative disorders and metabolic syndromes. Mutations or dysregulation of ATPAF1 have been linked to impaired mitochondrial function, leading to reduced ATP production and increased oxidative stress. Understanding the structure and function of ATPAF1, particularly its reassembly into the ATP synthase complex, can provide insights into mitochondrial pathophysiology. In recent years, advances in recombinant protein technology have facilitated the production and purification of ATPAF1, allowing researchers to probe its biochemical properties and interactions. Such studies are vital for elucidating the molecular mechanisms by which ATPAF1 modulates ATP synthase activity and overall mitochondrial function, potentially revealing new therapeutic targets for conditions associated with mitochondrial dysfunction. As the field evolves, the exploration of ATPAF1 restructured in vitro offers exciting prospects for enhancing our comprehension of energy metabolism at the cellular level.
