Analytical Data
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基因名
troA
- Application
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别名
Tromp-1 (troMP1)
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种属
Treponema pallidum
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P96116
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表达区间
23-308aa
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分子量
38.2 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
The study of troA recombinant protein centers around its role in bacterial physiology and antibiotic resistance. TroA, or the "transition metal transport protein A," is crucial for the uptake of essential metal ions, such as zinc and manganese, which are vital for various enzymatic processes and maintain cellular homeostasis in bacteria. Researchers have identified that bacteria, including pathogens, often rely on metal acquisition systems like troA to thrive in the host environment and evade immune responses. Moreover, understanding the molecular mechanisms by which troA mediates metal transport could provide insights into bacterial survival strategies and contribute to the development of novel antimicrobial therapies. By producing troA as a recombinant protein, scientists aim to elucidate its structural and functional properties, investigate its interactions with metal ions, and explore its potential as a target for drug design. This research not only enhances our understanding of bacterial nutrient acquisition but also holds promise for addressing the pressing challenge of antibiotic resistance in medical microbiology.
