Analytical Data
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Gene name
ATP5F1
- Application
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Alternative Names
ATP5F1;ATP5F1;ATP synthase F(0) complex subunit B1. 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
P24539
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Expression Region
1-256aa
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AA Sequence
MESPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELG LEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAV LDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVT HPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYI AWPLQGWQATFGGGDHPPKSDLEVLFQGPLETSLYKKAGTMLSRVVLSAA ATAAPSLKNAAFLGPGVLQATRTFHTGQPHLVPVPPLPEYGGKVRYGLIP EEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETFTALSVLGVMV YGIKKYGPFVADFADKLNEQKLAQLEEAKQASIQHIQNAIDTEKSQQALV QKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYHISVQNMMRRK EQEHMINWVEKHVVQSISTQQEKETIAKCIADLKLLAKKAQAQPVM
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Molecular Weight
55 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
Related Products
Protein Description
ATP5F1, also known as ATP synthase F1 complex, plays a crucial role in cellular energy production by synthesizing adenosine triphosphate (ATP) in mitochondria. Research on ATP5F1 recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. The F1 sector of ATP synthase consists of multiple subunits, and recombinant expression allows for the study of their structure, function, and interactions in detail. Understanding the dynamics of ATP5F1 is essential for elucidating the mechanisms of oxidative phosphorylation and ATP production, which are vital for cellular metabolism. Additionally, altered expression or mutations in ATP5F1 have been implicated in various mitochondrial diseases and metabolic disorders. By producing recombinant ATP5F1, researchers can investigate its role in these diseases, develop potential therapeutic strategies, and explore the protein's properties for industrial applications, such as in bioenergy. Overall, the study of ATP5F1 recombinant proteins is pivotal for advancing our knowledge of mitochondrial function and addressing related health challenges.











