Analytical Data
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基因名
MT-ATP6
- Application
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别名
(F-ATPase protein 6)
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种属
Chicken
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P14092
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表达区间
1-227aa
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分子量
26.3 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
MT-ATP6, a crucial component of the mitochondrial ATP synthase complex, plays a vital role in mitochondrial energy production. It encodes a subunit of ATP synthase located in the inner mitochondrial membrane, essential for ATP generation through oxidative phosphorylation. Research on MT-ATP6 has gained momentum due to its implications in various mitochondrial diseases and conditions, including neurodegenerative diseases, diabetes, and aging. Mutations in the MT-ATP6 gene have been linked to several pathogenic phenotypes, resulting in energy deficiency and contributing to the onset of mitochondrial disorders. The study of recombinant MT-ATP6 proteins enables researchers to explore the functional consequences of these mutations and their effects on ATP synthase activity. Additionally, understanding the structure and dynamics of MT-ATP6 is critical for developing therapeutic strategies aimed at restoring mitochondrial function in affected patients. Advances in recombinant protein expression and purification techniques have facilitated the detailed investigation of this protein, thereby providing insights into its role in bioenergetics and mitochondrial pathophysiology. This research not only enhances our comprehension of mitochondrial biology but also holds promise for developing innovative treatments for a spectrum of mitochondrial-related diseases. Overall, the continued exploration of MT-ATP6 and its recombinant forms is essential for elucidating the mechanisms of mitochondrial dysfunction and advancing potential therapeutic interventions.












