Analytical Data
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基因名
cyp125
- Application
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别名
cyp125；cyp125A1；Steroid C26-monooxygenase
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P9WPP1
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表达区间
1-433aa
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氨基酸序列
MSWNHQSVEIAVRRTTVPSPNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPGKGGGFHDGGFWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLNMDAPHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVEQVSCELPLQAIAGLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSAELIGYAMKMAEEKAKNPADDIVTQLIQADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITQGMMAFAEHPDQWELYKKVRPETAADEIVRWATPVTAFQRTALRDYELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNILRNPNPHVGFGGTGAHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIKHWQVDYTGRCPVAH
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分子量
54.5 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
CYP125 is a member of the cytochrome P450 superfamily, which plays a crucial role in the metabolism of various substrates, including drugs, steroids, and fatty acids. The study of CYP125 has garnered attention due to its distinct substrate specificity and its potential applications in bioremediation and drug development. This enzyme, originally isolated from certain bacterial species, exhibits notable catalytic efficiency and stability, making it an attractive candidate for further research. Understanding the structure-function relationship of CYP125 can provide insights into its unique enzymatic mechanisms and facilitate the engineering of this protein for enhanced performance in industrial applications. Additionally, the exploration of CYP125's interactions with different substrates can reveal novel pathways for drug metabolism, ultimately contributing to advancements in pharmacology. The recombinant expression of CYP125 allows for detailed studies of its activity and regulation, paving the way for innovations in metabolic engineering and synthetic biology. Thus, the ongoing research into CYP125 and its recombinant protein forms holds significant promise for both fundamental science and practical applications in biotechnology.
